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https://www.cazypedia.org/api.php?action=feedcontributions&feedformat=atom&user=Peter+Reilly CAZypedia - User contributions [en-ca] 2026-05-03T17:32:41Z User contributions MediaWiki 1.35.10 https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=6176 Glycoside Hydrolase Family 44 2011-01-17T05:11:46Z

<p>Peter Reilly: /* References */</p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but <br>Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2009</cite><br> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu<br>Catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate <cite>Najmudin2006 Warner2011</cite>.<br /> <br /> == Kinetics and Mechanism ==<br /> The most complete analyses of kinetics on various substrates are by Najmudin et al. <cite>Najmudin2006</cite> and by Warner et al. <cite>Warner2010 Warner2011</cite>. GH44 endoglucanases are also xyloglucanases. They hydrolyze longer cellooligosaccharides faster than shorter cellooligosaccharides <cite>Warner2010 Warner2011</cite>. They act asymmetrically on cellooligosaccharides, for instance producing more cellobiose and cellotetraose than cellotriose from cellohexaose <cite>Warner2010 Warner2011</cite>, with substrates bound with more of their residues in negatively-numbered than in positively-numbered subsites. Furthermore, disproportionation occurs, with more cellotetraose than cellobiose formed from cellohexaose, evidently caused by formation of larger unobserved products that are then rapidly hydrolyzed <cite>Warner2010 Warner2011</cite>. The mechanism is retaining <cite>Kitago2007</cite>, with a covalent bond being formed between the catalytic nucleophile and the C1' atom, leading to cleavage of the aglycon. A second, double-displacement, step is the cleavage of the covalent bond by water.<br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 by soaking the wild-type crystals with cellopentaose or cellohexaose and noting the positions of the residues relative to the reducing end of the cellotetraose product <cite>Kitago2007</cite>, and also by finding no activity with E186Q and E359Q mutants. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 by location in the active site of the wild-type crystal structure <cite>Nam2009</cite>. ''Clostridium acetobutylicum'' xyloglucanase/endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 also by location in the crystal structure of the wild-type enzyme, and by comparison with the ''C. thermocellum'' structure <cite>Warner2010</cite>.<br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. <cite>Kitago2007</cite>, who found a TIM-like barrel domain and a beta-sandwich domain in ''C. thermocellum'' endoglucanase. Similar structures were found by Nam et al. <cite>Nam2009</cite> in a protein from a metagenomic library and by Warner et al. <cite>Warner2010</cite> in ''C. acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands <cite>Kitago2007</cite>.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. <cite>Kitago2007</cite> found that ''C. thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. <cite>Kitago2007</cite> of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2009 pmid=19345197<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010 pmid=19915043<br /> #Warner2011 Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. ''Kinetic characterization of a glycoside hydrolase family 44 xyloglucanase/endoglucanase from Ruminococcus flavefaciens FD-1''. Enzyme Microb Technol 2011 Jan 5; 48 (1) 27-32. doi:10.1016/j.enzmictec.2010.08.009 pmid: .<br /> </biblio><br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=6175 Glycoside Hydrolase Family 44 2011-01-17T05:11:06Z

<p>Peter Reilly: /* References */</p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but <br>Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2009</cite><br> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu<br>Catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate <cite>Najmudin2006 Warner2011</cite>.<br /> <br /> == Kinetics and Mechanism ==<br /> The most complete analyses of kinetics on various substrates are by Najmudin et al. <cite>Najmudin2006</cite> and by Warner et al. <cite>Warner2010 Warner2011</cite>. GH44 endoglucanases are also xyloglucanases. They hydrolyze longer cellooligosaccharides faster than shorter cellooligosaccharides <cite>Warner2010 Warner2011</cite>. They act asymmetrically on cellooligosaccharides, for instance producing more cellobiose and cellotetraose than cellotriose from cellohexaose <cite>Warner2010 Warner2011</cite>, with substrates bound with more of their residues in negatively-numbered than in positively-numbered subsites. Furthermore, disproportionation occurs, with more cellotetraose than cellobiose formed from cellohexaose, evidently caused by formation of larger unobserved products that are then rapidly hydrolyzed <cite>Warner2010 Warner2011</cite>. The mechanism is retaining <cite>Kitago2007</cite>, with a covalent bond being formed between the catalytic nucleophile and the C1' atom, leading to cleavage of the aglycon. A second, double-displacement, step is the cleavage of the covalent bond by water.<br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 by soaking the wild-type crystals with cellopentaose or cellohexaose and noting the positions of the residues relative to the reducing end of the cellotetraose product <cite>Kitago2007</cite>, and also by finding no activity with E186Q and E359Q mutants. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 by location in the active site of the wild-type crystal structure <cite>Nam2009</cite>. ''Clostridium acetobutylicum'' xyloglucanase/endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 also by location in the crystal structure of the wild-type enzyme, and by comparison with the ''C. thermocellum'' structure <cite>Warner2010</cite>.<br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. <cite>Kitago2007</cite>, who found a TIM-like barrel domain and a beta-sandwich domain in ''C. thermocellum'' endoglucanase. Similar structures were found by Nam et al. <cite>Nam2009</cite> in a protein from a metagenomic library and by Warner et al. <cite>Warner2010</cite> in ''C. acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands <cite>Kitago2007</cite>.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. <cite>Kitago2007</cite> found that ''C. thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. <cite>Kitago2007</cite> of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2009 pmid=19345197<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010 pmid=19915043<br /> #Warner2011 Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2011. ''Kinetic characterization of a glycoside hydrolase family 44 xyloglucanase/endoglucanase from Ruminococcus flavefaciens FD-1''. Enzyme Microb Technol 2011 Jan 5; 48 (1) 27-32. doi:10.1016/j.enzmictec.2010.08.009 pmid: .<br /> </biblio><br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=6174 Glycoside Hydrolase Family 44 2011-01-17T05:07:17Z

<p>Peter Reilly: /* Catalytic Residues */</p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but <br>Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2009</cite><br> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu<br>Catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate <cite>Najmudin2006 Warner2011</cite>.<br /> <br /> == Kinetics and Mechanism ==<br /> The most complete analyses of kinetics on various substrates are by Najmudin et al. <cite>Najmudin2006</cite> and by Warner et al. <cite>Warner2010 Warner2011</cite>. GH44 endoglucanases are also xyloglucanases. They hydrolyze longer cellooligosaccharides faster than shorter cellooligosaccharides <cite>Warner2010 Warner2011</cite>. They act asymmetrically on cellooligosaccharides, for instance producing more cellobiose and cellotetraose than cellotriose from cellohexaose <cite>Warner2010 Warner2011</cite>, with substrates bound with more of their residues in negatively-numbered than in positively-numbered subsites. Furthermore, disproportionation occurs, with more cellotetraose than cellobiose formed from cellohexaose, evidently caused by formation of larger unobserved products that are then rapidly hydrolyzed <cite>Warner2010 Warner2011</cite>. The mechanism is retaining <cite>Kitago2007</cite>, with a covalent bond being formed between the catalytic nucleophile and the C1' atom, leading to cleavage of the aglycon. A second, double-displacement, step is the cleavage of the covalent bond by water.<br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 by soaking the wild-type crystals with cellopentaose or cellohexaose and noting the positions of the residues relative to the reducing end of the cellotetraose product <cite>Kitago2007</cite>, and also by finding no activity with E186Q and E359Q mutants. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 by location in the active site of the wild-type crystal structure <cite>Nam2009</cite>. ''Clostridium acetobutylicum'' xyloglucanase/endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 also by location in the crystal structure of the wild-type enzyme, and by comparison with the ''C. thermocellum'' structure <cite>Warner2010</cite>.<br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. <cite>Kitago2007</cite>, who found a TIM-like barrel domain and a beta-sandwich domain in ''C. thermocellum'' endoglucanase. Similar structures were found by Nam et al. <cite>Nam2009</cite> in a protein from a metagenomic library and by Warner et al. <cite>Warner2010</cite> in ''C. acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands <cite>Kitago2007</cite>.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. <cite>Kitago2007</cite> found that ''C. thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. <cite>Kitago2007</cite> of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2009 pmid=19345197<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010 pmid=19915043<br /> #Warner2011 Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010. ''Kinetic characterization of a glycoside hydrolase family 44 xyloglucanase/endoglucanase from Ruminococcus flavefaciens FD-1''. Enzyme Microb Technol 2011 Jan 5; 48 (1) 27-32. doi:10.1016/j.enzmictec.2010.08.009 pmid: .<br /> </biblio><br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=6173 Glycoside Hydrolase Family 44 2011-01-17T05:05:44Z

<p>Peter Reilly: /* References */</p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but <br>Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2009</cite><br> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu<br>Catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate <cite>Najmudin2006 Warner2011</cite>.<br /> <br /> == Kinetics and Mechanism ==<br /> The most complete analyses of kinetics on various substrates are by Najmudin et al. <cite>Najmudin2006</cite> and by Warner et al. <cite>Warner2010 Warner2011</cite>. GH44 endoglucanases are also xyloglucanases. They hydrolyze longer cellooligosaccharides faster than shorter cellooligosaccharides <cite>Warner2010 Warner2011</cite>. They act asymmetrically on cellooligosaccharides, for instance producing more cellobiose and cellotetraose than cellotriose from cellohexaose <cite>Warner2010 Warner2011</cite>, with substrates bound with more of their residues in negatively-numbered than in positively-numbered subsites. Furthermore, disproportionation occurs, with more cellotetraose than cellobiose formed from cellohexaose, evidently caused by formation of larger unobserved products that are then rapidly hydrolyzed <cite>Warner2010 Warner2011</cite>. The mechanism is retaining <cite>Kitago2007</cite>, with a covalent bond being formed between the catalytic nucleophile and the C1' atom, leading to cleavage of the aglycon. A second, double-displacement, step is the cleavage of the covalent bond by water.<br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 by soaking the wild-type crystals with cellopentaose or cellohexaose and noting the positions of the residues relative to the reducing end of the cellotetraose product <cite>Kitago2007</cite>, and also by finding no activity with E186Q and E359Q mutants. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 by location in the active site of the wild-type crystal structure <cite>Nam2009</cite>.''Clostridium acetobutylicum'' xyloglucanase/endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 also by location in the crystal structure of the wild-type enzyme, and by comparison with the ''C. thermocellum'' structure <cite>Warner2010</cite>.<br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. <cite>Kitago2007</cite>, who found a TIM-like barrel domain and a beta-sandwich domain in ''C. thermocellum'' endoglucanase. Similar structures were found by Nam et al. <cite>Nam2009</cite> in a protein from a metagenomic library and by Warner et al. <cite>Warner2010</cite> in ''C. acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands <cite>Kitago2007</cite>.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. <cite>Kitago2007</cite> found that ''C. thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. <cite>Kitago2007</cite> of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2009 pmid=19345197<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010 pmid=19915043<br /> #Warner2011 Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010. ''Kinetic characterization of a glycoside hydrolase family 44 xyloglucanase/endoglucanase from Ruminococcus flavefaciens FD-1''. Enzyme Microb Technol 2011 Jan 5; 48 (1) 27-32. doi:10.1016/j.enzmictec.2010.08.009 pmid: .<br /> </biblio><br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=6172 Glycoside Hydrolase Family 44 2011-01-17T05:00:33Z

<p>Peter Reilly: /* Catalytic Residues */</p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but <br>Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2009</cite><br> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu<br>Catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate <cite>Najmudin2006 Warner2011</cite>.<br /> <br /> == Kinetics and Mechanism ==<br /> The most complete analyses of kinetics on various substrates are by Najmudin et al. <cite>Najmudin2006</cite> and by Warner et al. <cite>Warner2010 Warner2011</cite>. GH44 endoglucanases are also xyloglucanases. They hydrolyze longer cellooligosaccharides faster than shorter cellooligosaccharides <cite>Warner2010 Warner2011</cite>. They act asymmetrically on cellooligosaccharides, for instance producing more cellobiose and cellotetraose than cellotriose from cellohexaose <cite>Warner2010 Warner2011</cite>, with substrates bound with more of their residues in negatively-numbered than in positively-numbered subsites. Furthermore, disproportionation occurs, with more cellotetraose than cellobiose formed from cellohexaose, evidently caused by formation of larger unobserved products that are then rapidly hydrolyzed <cite>Warner2010 Warner2011</cite>. The mechanism is retaining <cite>Kitago2007</cite>, with a covalent bond being formed between the catalytic nucleophile and the C1' atom, leading to cleavage of the aglycon. A second, double-displacement, step is the cleavage of the covalent bond by water.<br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 by soaking the wild-type crystals with cellopentaose or cellohexaose and noting the positions of the residues relative to the reducing end of the cellotetraose product <cite>Kitago2007</cite>, and also by finding no activity with E186Q and E359Q mutants. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 by location in the active site of the wild-type crystal structure <cite>Nam2009</cite>.''Clostridium acetobutylicum'' xyloglucanase/endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 also by location in the crystal structure of the wild-type enzyme, and by comparison with the ''C. thermocellum'' structure <cite>Warner2010</cite>.<br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. <cite>Kitago2007</cite>, who found a TIM-like barrel domain and a beta-sandwich domain in ''C. thermocellum'' endoglucanase. Similar structures were found by Nam et al. <cite>Nam2009</cite> in a protein from a metagenomic library and by Warner et al. <cite>Warner2010</cite> in ''C. acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands <cite>Kitago2007</cite>.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. <cite>Kitago2007</cite> found that ''C. thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. <cite>Kitago2007</cite> of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2009 pmid=19345197<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010 pmid=19915043<br /> #Warner2011 Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010. ''Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from Ruminococcus flavefaciens FD-1''. Enzyme Microb Technol 2011 Jan 5; 48 (1) 27-32. doi:10.1016/j.enzmictec.2010.08.009 pmid: .<br /> </biblio><br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=6171 Glycoside Hydrolase Family 44 2011-01-17T04:58:53Z

<p>Peter Reilly: /* Catalytic Residues */</p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but <br>Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2009</cite><br> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu<br>Catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate <cite>Najmudin2006 Warner2011</cite>.<br /> <br /> == Kinetics and Mechanism ==<br /> The most complete analyses of kinetics on various substrates are by Najmudin et al. <cite>Najmudin2006</cite> and by Warner et al. <cite>Warner2010 Warner2011</cite>. GH44 endoglucanases are also xyloglucanases. They hydrolyze longer cellooligosaccharides faster than shorter cellooligosaccharides <cite>Warner2010 Warner2011</cite>. They act asymmetrically on cellooligosaccharides, for instance producing more cellobiose and cellotetraose than cellotriose from cellohexaose <cite>Warner2010 Warner2011</cite>, with substrates bound with more of their residues in negatively-numbered than in positively-numbered subsites. Furthermore, disproportionation occurs, with more cellotetraose than cellobiose formed from cellohexaose, evidently caused by formation of larger unobserved products that are then rapidly hydrolyzed <cite>Warner2010 Warner2011</cite>. The mechanism is retaining <cite>Kitago2007</cite>, with a covalent bond being formed between the catalytic nucleophile and the C1' atom, leading to cleavage of the aglycon. A second, double-displacement, step is the cleavage of the covalent bond by water.<br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 by soaking the wild-type crystals with cellopentaose or cellohexaose and noting the positions of the residues relative to the reducing end of the cellotetraose product <cite>Kitago2007</cite>, and also by finding no activity with E186Q and E359Q mutants. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 by location in the active site of the wild-type crystal structure <cite>Nam2009</cite>.''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 also by location in the crystal structure of the wild-type enzyme, and by comparison with the ''C. thermocellum'' structure <cite>Warner2010</cite>.<br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. <cite>Kitago2007</cite>, who found a TIM-like barrel domain and a beta-sandwich domain in ''C. thermocellum'' endoglucanase. Similar structures were found by Nam et al. <cite>Nam2009</cite> in a protein from a metagenomic library and by Warner et al. <cite>Warner2010</cite> in ''C. acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands <cite>Kitago2007</cite>.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. <cite>Kitago2007</cite> found that ''C. thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. <cite>Kitago2007</cite> of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2009 pmid=19345197<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010 pmid=19915043<br /> #Warner2011 Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010. ''Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from Ruminococcus flavefaciens FD-1''. Enzyme Microb Technol 2011 Jan 5; 48 (1) 27-32. doi:10.1016/j.enzmictec.2010.08.009 pmid: .<br /> </biblio><br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=6170 Glycoside Hydrolase Family 44 2011-01-17T04:55:40Z

<p>Peter Reilly: /* References */</p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but <br>Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2009</cite><br> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu<br>Catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate <cite>Najmudin2006 Warner2011</cite>.<br /> <br /> == Kinetics and Mechanism ==<br /> The most complete analyses of kinetics on various substrates are by Najmudin et al. <cite>Najmudin2006</cite> and by Warner et al. <cite>Warner2010 Warner2011</cite>. GH44 endoglucanases are also xyloglucanases. They hydrolyze longer cellooligosaccharides faster than shorter cellooligosaccharides <cite>Warner2010 Warner2011</cite>. They act asymmetrically on cellooligosaccharides, for instance producing more cellobiose and cellotetraose than cellotriose from cellohexaose <cite>Warner2010 Warner2011</cite>, with substrates bound with more of their residues in negatively-numbered than in positively-numbered subsites. Furthermore, disproportionation occurs, with more cellotetraose than cellobiose formed from cellohexaose, evidently caused by formation of larger unobserved products that are then rapidly hydrolyzed <cite>Warner2010 Warner2011</cite>. The mechanism is retaining <cite>Kitago2007</cite>, with a covalent bond being formed between the catalytic nucleophile and the C1' atom, leading to cleavage of the aglycon. A second, double-displacement, step is the cleavage of the covalent bond by water.<br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 by soaking the wild-type crystals with cellopentaose or cellohexaose and noting the their position relative to the reducing end of the cellotetraose product <cite>Kitago2007</cite>, and also by finding no activity with E186Q and E359Q mutants. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 by location in the active site of the wild-type crystal structure <cite>Nam2009</cite>.''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 also by location in the crystal structure of the wild-type enzyme, and by comparison with the ''C. thermocellum'' structure <cite>Warner2010</cite>.<br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. <cite>Kitago2007</cite>, who found a TIM-like barrel domain and a beta-sandwich domain in ''C. thermocellum'' endoglucanase. Similar structures were found by Nam et al. <cite>Nam2009</cite> in a protein from a metagenomic library and by Warner et al. <cite>Warner2010</cite> in ''C. acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands <cite>Kitago2007</cite>.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. <cite>Kitago2007</cite> found that ''C. thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. <cite>Kitago2007</cite> of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2009 pmid=19345197<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010 pmid=19915043<br /> #Warner2011 Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010. ''Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from Ruminococcus flavefaciens FD-1''. Enzyme Microb Technol 2011 Jan 5; 48 (1) 27-32. doi:10.1016/j.enzmictec.2010.08.009 pmid: .<br /> </biblio><br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=6169 Glycoside Hydrolase Family 44 2011-01-17T04:54:11Z

<p>Peter Reilly: /* Catalytic Residues */</p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but <br>Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2009</cite><br> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu<br>Catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate <cite>Najmudin2006 Warner2011</cite>.<br /> <br /> == Kinetics and Mechanism ==<br /> The most complete analyses of kinetics on various substrates are by Najmudin et al. <cite>Najmudin2006</cite> and by Warner et al. <cite>Warner2010 Warner2011</cite>. GH44 endoglucanases are also xyloglucanases. They hydrolyze longer cellooligosaccharides faster than shorter cellooligosaccharides <cite>Warner2010 Warner2011</cite>. They act asymmetrically on cellooligosaccharides, for instance producing more cellobiose and cellotetraose than cellotriose from cellohexaose <cite>Warner2010 Warner2011</cite>, with substrates bound with more of their residues in negatively-numbered than in positively-numbered subsites. Furthermore, disproportionation occurs, with more cellotetraose than cellobiose formed from cellohexaose, evidently caused by formation of larger unobserved products that are then rapidly hydrolyzed <cite>Warner2010 Warner2011</cite>. The mechanism is retaining <cite>Kitago2007</cite>, with a covalent bond being formed between the catalytic nucleophile and the C1' atom, leading to cleavage of the aglycon. A second, double-displacement, step is the cleavage of the covalent bond by water.<br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 by soaking the wild-type crystals with cellopentaose or cellohexaose and noting the their position relative to the reducing end of the cellotetraose product <cite>Kitago2007</cite>, and also by finding no activity with E186Q and E359Q mutants. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 by location in the active site of the wild-type crystal structure <cite>Nam2009</cite>.''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 also by location in the crystal structure of the wild-type enzyme, and by comparison with the ''C. thermocellum'' structure <cite>Warner2010</cite>.<br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. <cite>Kitago2007</cite>, who found a TIM-like barrel domain and a beta-sandwich domain in ''C. thermocellum'' endoglucanase. Similar structures were found by Nam et al. <cite>Nam2009</cite> in a protein from a metagenomic library and by Warner et al. <cite>Warner2010</cite> in ''C. acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands <cite>Kitago2007</cite>.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. <cite>Kitago2007</cite> found that ''C. thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. <cite>Kitago2007</cite> of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2010 pmid=19345197<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010 pmid=19915043<br /> #Warner2011 Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010. ''Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from Ruminococcus flavefaciens FD-1''. Enzyme Microb Technol 2011 Jan 5; 48 (1) 27-32. doi:10.1016/j.enzmictec.2010.08.009 pmid: .<br /> </biblio><br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=6168 Glycoside Hydrolase Family 44 2011-01-17T04:50:08Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but <br>Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2009</cite><br> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu<br>Catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate <cite>Najmudin2006 Warner2011</cite>.<br /> <br /> == Kinetics and Mechanism ==<br /> The most complete analyses of kinetics on various substrates are by Najmudin et al. <cite>Najmudin2006</cite> and by Warner et al. <cite>Warner2010 Warner2011</cite>. GH44 endoglucanases are also xyloglucanases. They hydrolyze longer cellooligosaccharides faster than shorter cellooligosaccharides <cite>Warner2010 Warner2011</cite>. They act asymmetrically on cellooligosaccharides, for instance producing more cellobiose and cellotetraose than cellotriose from cellohexaose <cite>Warner2010 Warner2011</cite>, with substrates bound with more of their residues in negatively-numbered than in positively-numbered subsites. Furthermore, disproportionation occurs, with more cellotetraose than cellobiose formed from cellohexaose, evidently caused by formation of larger unobserved products that are then rapidly hydrolyzed <cite>Warner2010 Warner2011</cite>. The mechanism is retaining <cite>Kitago2007</cite>, with a covalent bond being formed between the catalytic nucleophile and the C1' atom, leading to cleavage of the aglycon. A second, double-displacement, step is the cleavage of the covalent bond by water.<br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 by soaking the wild-type crystals with cellopentaose or cellohexaose and noting the their position relative to the reducting end of the cellotetraose product <cite>Kitago2007</cite>, and also by finding no activity with E186Q and E359Q mutants. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 by location in the active site of the wild-type crystal structure <cite>Nam2009</cite>.''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 also by location in the crystal structure of the wild-type enzyme, and by comparison with the ''C. thermocellum'' structure <cite>Warner2010</cite>.<br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. <cite>Kitago2007</cite>, who found a TIM-like barrel domain and a beta-sandwich domain in ''C. thermocellum'' endoglucanase. Similar structures were found by Nam et al. <cite>Nam2009</cite> in a protein from a metagenomic library and by Warner et al. <cite>Warner2010</cite> in ''C. acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands <cite>Kitago2007</cite>.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. <cite>Kitago2007</cite> found that ''C. thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. <cite>Kitago2007</cite> of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2010 pmid=19345197<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010 pmid=19915043<br /> #Warner2011 Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010. ''Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from Ruminococcus flavefaciens FD-1''. Enzyme Microb Technol 2011 Jan 5; 48 (1) 27-32. doi:10.1016/j.enzmictec.2010.08.009 pmid: .<br /> </biblio><br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=6163 Glycoside Hydrolase Family 44 2011-01-05T21:29:31Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but <br>Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2010</cite><br> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu<br>Catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate <cite>Najmudin2006 Warner2010b</cite>.<br /> <br /> == Kinetics and Mechanism ==<br /> The most complete analyses of kinetics on various substrates are by Najmudin et al. <cite>Najmudin2006</cite> and by Warner et al. <cite>Warner2010b Warner2010a</cite>. GH44 endoglucanases are also xyloglucanases. They hydrolyze longer cellooligosaccharides faster than shorter cellooligosaccharides <cite>Warner2010b Warner2010a</cite>. They act asymmetrically on cellooligosaccharides, for instance producing more cellobiose and cellotetraose than cellotriose from cellohexaose <cite>Warner2010b Warner2010a</cite>, with substrates bound with more of their residues in negatively-numbered than in positively-numbered subsites. Furthermore, disproportionation occurs, with more cellotetraose than cellobiose formed from cellohexaose, evidently caused by formation of larger unobserved products that are then rapidly hydrolyzed <cite>Warner2010b Warner2010a</cite>. The mechanism is retaining <cite>Kitago2007</cite>, with a covalent bond being formed between the catalytic nucleophile and the C1' atom, leading to cleavage of the aglycon. A second, double-displacement, step is the cleavage of the covalent bond by water.<br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 <cite>Kitago2007</cite>. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 <cite>Nam2010</cite>.''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 <cite>Warner2010a</cite>.<br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. <cite>Kitago2007</cite>, who found a TIM-like barrel domain and a beta-sandwich domain in ''C. thermocellum'' endoglucanase. Similar structures were found by Nam et al. <cite>Nam2010</cite> in a protein from a metagenomic library and by Warner et al. <cite>Warner2010a</cite> in ''C. acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands <cite>Kitago2007</cite>.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. <cite>Kitago2007</cite> found that ''C. thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. <cite>Kitago2007</cite> of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2010 pmid=19345197<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010b Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010. ''Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from Ruminococcus flavefaciens FD-1''. Enzyme Microb Technol 2011 Jan 5; 48 (1) 27-32. doi:10.1016/j.enzmictec.2010.08.009 pmid: .<br /> #Warner2010a pmid=19915043<br /> </biblio><br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5633 Glycoside Hydrolase Family 44 2010-08-24T04:29:26Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2010</cite> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate <cite>Najmudin2006</cite>,<cite>Warner2010b</cite>.<br /> <br /> <br /> == Kinetics and Mechanism ==<br /> The most complete analyses of kinetics on various substrates are by Najmudin et al. <cite>Najmudin2006</cite> and by Warner et al. <cite>Warner2010b</cite>,<cite>Warner2010a</cite>. GH44 endoglucanases are also xyloglucanases. They hydrolyze longer cellooligosaccharides faster than shorter cellooligosaccharides <cite>Warner2010b</cite>,<cite>Warner2010a</cite>. They act asymmetrically on cellooligosaccharides, for instance producing more cellobiose and cellotetraose than cellotriose from cellohexaose <cite>Warner2010b</cite>,<cite>Warner2010a</cite>, with substrates bound with more of their residues in negatively-numbered than in positively-numbered subsites. Furthermore, disproportionation occurs, with more cellotetraose than cellobiose formed from cellohexaose, evidently caused by formation of larger unobserved products that are then rapidly hydrolyzed <cite>Warner2010b</cite>,<cite>Warner2010a</cite>. The mechanism is retaining <cite>Kitago2007</cite>, with a covalent bond being formed between the catalytic nucleophile and the C1' atom, leading to cleavage of the aglycon. A second, double-displacement, step is the cleavage of the covalent bond by water.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 <cite>Kitago2007</cite>. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 <cite>Nam2010</cite>.''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 <cite>Warner2010a</cite>.<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. <cite>Kitago2007</cite>, who found a TIM-like barrel domain and a beta-sandwich domain in ''C. thermocellum'' endoglucanase. Similar structures were found by Nam et al. <cite>Nam2010</cite> in a protein from a metagenomic library and by Warner et al. <cite>Warner2010a</cite> in ''C. acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands <cite>Kitago2007</cite>.<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. <cite>Kitago2007</cite> found that ''C. thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. <cite>Kitago2007</cite> of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2010 pmid=19345197<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010b Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010. ''Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from Ruminococcus flavefaciens FD-1''. Submitted for publication.<br /> #Warner2010a pmid=19915043<br /> </biblio><br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5632 Glycoside Hydrolase Family 44 2010-08-24T04:28:08Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2010</cite> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate <cite>Najmudin2006</cite>,<cite>Warner2010b</cite>.<br /> <br /> <br /> == Kinetics and Mechanism ==<br /> The most complete analyses of kinetics on various substrates are by Najmudin et al. <cite>Najmudin2006</cite> and by Warner et al. <cite>Warner2010a</cite>,<cite>Warner2010b</cite>. GH44 endoglucanases are also xyloglucanases. They hydrolyze longer cellooligosaccharides faster than shorter cellooligosaccharides <cite>Warner2010a</cite>,<cite>Warner2010b</cite>. They act asymmetrically on cellooligosaccharides, for instance producing more cellobiose and cellotetraose than cellotriose from cellohexaose <cite>Warner2010a</cite>,<cite>Warner2010b</cite>, with substrates bound with more of their residues in negatively-numbered than in positively-numbered subsites. Furthermore, disproportionation occurs, with more cellotetraose than cellobiose formed from cellohexaose, evidently caused by formation of larger unobserved products that are then rapidly hydrolyzed <cite>Warner2010a</cite>,<cite>Warner2010b</cite>. The mechanism is retaining <cite>Kitago2007</cite>, with a covalent bond being formed between the catalytic nucleophile and the C1' atom, leading to cleavage of the aglycon. A second, double-displacement, step is the cleavage of the covalent bond by water.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 <cite>Kitago2007</cite>. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 <cite>Nam2010</cite>.''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 <cite>Warner2010a</cite>.<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. <cite>Kitago2007</cite>, who found a TIM-like barrel domain and a beta-sandwich domain in ''C. thermocellum'' endoglucanase. Similar structures were found by Nam et al. <cite>Nam2010</cite> in a protein from a metagenomic library and by Warner et al. <cite>Warner2010a</cite> in ''C. acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands <cite>Kitago2007</cite>.<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. <cite>Kitago2007</cite> found that ''C. thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. <cite>Kitago2007</cite> of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2010 pmid=19345197<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010b Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010. ''Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from Ruminococcus flavefaciens FD-1''. Submitted for publication.<br /> #Warner2010a pmid=19915043<br /> </biblio><br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5631 Glycoside Hydrolase Family 44 2010-08-24T04:25:45Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2010</cite> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate <cite>Najmudin2006</cite>,<cite>Warner2010b</cite>.<br /> <br /> <br /> == Kinetics and Mechanism ==<br /> The most complete analyses of kinetics on various substrates are by Najmudin et al. <cite>Najmudin2006</cite> and by Warner et al. <cite>Warner2010a</cite>,<cite>Warner2010b</cite>. GH44 endoglucanases are also xyloglucanases. They hydrolyze longer cellooligosaccharides faster than shorter cellooligosaccharides <cite>Warner2010a</cite>,<cite>Warner2010b</cite>. They act asymmetrically on cellooligosaccharides, for instance producing more cellobiose and cellotetraose than cellotriose from cellohexaose <cite>Warner2010a</cite>,<cite>Warner2010b</cite>, with substrates bound with more of their residues in negatively-numbered than in positively-numbered subsites. Furthermore, disproportionation occurs, with more cellotetraose than cellobiose formed from cellohexaose, evidently caused by formation of larger unobserved products that are then rapidly hydrolyzed <cite>Warner2010a</cite>,<cite>Warner2010b</cite>. The mechanism is retaining <cite>Kitago2007</cite>, with a covalent bond being formed between the catalytic nucleophile and the C1' atom, leading to cleavage of the aglycon. A second, double-displacement, step is the cleavage of the covalent bond by water.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 <cite>Kitago2007</cite>. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 <cite>Nam2010</cite>.''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 <cite>Warner2010a</cite>.<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. <cite>Kitago2007</cite>, who found a TIM-like barrel domain and a beta-sandwich domain in ''C. thermocellum'' endoglucanase. Similar structures were found by Nam et al. <cite>Nam2010</cite> in a protein from a metagenomic library and by Warner et al. <cite>Warner2010a</cite> in ''C. acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands <cite>Kitago2007</cite>.<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. <cite>Kitago2007</cite> found that ''C. thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. <cite>Kitago2007</cite> of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2010 pmid=19345197<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010a pmid=19915043<br /> #Warner2010b Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010. ''Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from Ruminococcus flavefaciens FD-1''. Submitted for publication.<br /> </biblio><br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5630 Glycoside Hydrolase Family 44 2010-08-24T04:22:23Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2010</cite> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate <cite>Najmudin2006</cite>,<cite>Warner2010b</cite>.<br /> <br /> <br /> == Kinetics and Mechanism ==<br /> The most complete analysis of kinetics on various substrates is by Warner et al. <cite>Warner2010a</cite>,<cite>Warner2010b</cite> and by Najmudin et al. <cite>Najmudin2006</cite>. GH44 endoglucanases are also xyloglucanases. They hydrolyze longer cellooligosaccharides faster than shorter cellooligosaccharides <cite>Warner2010a</cite>,<cite>Warner2010b</cite>. They act asymmetrically on cellooligosaccharides, for instance producing more cellobiose and cellotetraose than cellotriose from cellohexaose <cite>Warner2010a</cite>,<cite>Warner2010b</cite>, with substrates bound with more of their residues in negatively-numbered than in positively-numbered subsites. Furthermore, disproportionation occurs, with more cellotetraose than cellobiose formed from cellohexaose, evidently caused by formation of larger unobserved products that are then rapidly hydrolyzed <cite>Warner2010a</cite>,<cite>Warner2010b</cite>. The mechanism is retaining <cite>Kitago2007</cite>, with a covalent bond being formed between the catalytic nucleophile and the C1' atom, leading to cleavage of the aglycon. A second, double-displacement, step is the cleavage of the covalent bond by water.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 <cite>Kitago2007</cite>. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 <cite>Nam2010</cite>.''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 <cite>Warner2010a</cite>.<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. <cite>Kitago2007</cite>, who found a TIM-like barrel domain and a beta-sandwich domain in ''C. thermocellum'' endoglucanase. Similar structures were found by Nam et al. <cite>Nam2010</cite> in a protein from a metagenomic library and by Warner et al. <cite>Warner2010a</cite> in ''C. acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands <cite>Kitago2007</cite>.<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. <cite>Kitago2007</cite> found that ''C. thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. <cite>Kitago2007</cite> of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2010 pmid=19345197<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010a pmid=19915043<br /> #Warner2010b Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010. ''Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from Ruminococcus flavefaciens FD-1''. Submitted for publication.<br /> </biblio><br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5629 Glycoside Hydrolase Family 44 2010-08-24T04:17:15Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2010</cite> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate <cite>Najmudin2006</cite>,<cite>Warner2010b</cite>.<br /> <br /> <br /> == Kinetics and Mechanism ==<br /> The most complete analysis of kinetics on various substrates is by Warner et al. <cite>Warner2010a</cite>,<cite>Warner2010b</cite> and by Najmudin et al. <cite>Najmudin2006</cite>. GH44 endoglucanases are also xyloglucanases. They hydrolyze longer cellooligosaccharides faster than shorter cellooligosaccharides <cite>Warner2010a</cite>,<cite>Warner2010b</cite>. They act asymmetrically on cellooligosaccharides, for instance producing more cellobiose and cellotetraose than cellotriose from cellohexaose <cite>Warner2010a</cite>,<cite>Warner2010b</cite>, with substrates bound with more of their residues in negatively-numbered than in positively-numbered subsites. Furthermore, disproportionation occurs, with more cellotetraose than cellobiose formed from cellohexaose, evidently caused by formation of larger unobserved products that are then rapidly hydrolyzed <cite>Warner2010a</cite>,<cite>Warner2010b</cite>. The mechanism is retaining <cite>Kitago2007</cite>, with a covalent bond being formed between the catalytic nucleophile and the C1' atom, leading to cleavage of the aglycon. A second, double-displacement, step is the cleavage of the covalent bond by water.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 <cite>Kitago2007</cite>. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 <cite>Nam2010</cite>.''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 <cite>Warner2010a</cite>.<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. <cite>Kitago2007</cite>, who found a TIM-like barrel domain and a beta-sandwich domain in ''C. thermocellum'' endoglucanase. Similar structures were found by Nam et al. <cite>Nam2010</cite> in a protein from a metagenomic library and by Warner et al. <cite>Warner2010a</cite> in ''C. acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands <cite>Kitago2007</cite>.<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. <cite>Kitago2007</cite> found that ''C. thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. <cite>Kitago2007</cite>, by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. <cite>Kitago2007</cite> of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2010 pmid=19345197<br /> #Warner2010a pmid=19915043<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010b Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010. ''Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from Ruminococcus flavefaciens FD-1''. Submitted for publication.<br /> </biblio><br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=User:Peter_Reilly&diff=5628 User:Peter Reilly 2010-08-24T04:01:58Z

<p>Peter Reilly: </p> <hr /> <div>[[Image:Reilly-Peter photo.jpg|200px|right]]<br /> <br /> Peter Reilly received an A.B. in chemistry from Princeton and a Ph.D. in chemical engineering from Pennsylvania. He worked at DuPont in New Jersey and then was an assistant professor of chemical engineering at the University of Nebraska–Lincoln. Since 1974 he has been at Iowa State University, where he is professor of chemical and biological engineering and Anson Marston Distinguished Professor in Engineering. His most extensive work in glycoside hydrolases, both experimental and computational, has been with glucoamylase ([[GH15]]). He and his students have also worked experimentally with [[GH10]], [[GH13]], [[GH43]], and [[GH44]] and computationally with [[GH1]], [[GH6]], [[GH7]], [[GH8]], [[GH14]], [[GH38]], [[GH43]], [[GH47]], and [[GH94]]. At present he and his students are developing ThYme, a database for thioester-active enzymes similar to CAZy.<br /> <br /> [[Category:Contributors|Reilly,Peter]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=File:Reilly-Peter_photo.jpg&diff=5627 File:Reilly-Peter photo.jpg 2010-08-24T03:57:18Z

<p>Peter Reilly: </p> <hr /> <div></div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5453 Glycoside Hydrolase Family 44 2010-08-15T01:33:18Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2010</cite> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate [4,5].<br /> <br /> <br /> == Kinetics and Mechanism ==<br /> The most complete analysis of kinetics on various substrates is by Warner et al. [3,5] and by Najmudin et al. [4]. GH44 endoglucanases are also xyloglucanases. They hydrolyze longer cellooligosaccharides faster than shorter cellooligosaccharides [3,5]. They act asymmetrically on cellooligosaccharides, for instance producing more cellobiose and cellotetraose than cellotriose from cellohexaose [3,5], with substrates bound with more of their residues in negatively-numbered than in positively-numbered subsites. Furthermore, disproportionation occurs, with more cellotetraose than cellobiose formed from cellohexaose, evidently caused by formation of larger unobserved products that are then rapidly hydrolyzed [3,5]. The mechanism is retaining [1], with a covalent bond being formed between the catalytic nucleophile and the C1' atom, leading to cleavage of the aglycon. A second, double-displacement, step is the cleavage of the covalent bond by water.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in ''C. thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and by Warner et al. [3] in ''C. acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. [1] found that ''C. thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. [1], by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. [1], by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. [1] of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2010 pmid=19345197<br /> #Warner2010a pmid=19915043<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010b Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010. ''Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from Ruminococcus flavefaciens FD-1''. Submitted for publication.<br /> </biblio><br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5452 Glycoside Hydrolase Family 44 2010-08-15T01:07:11Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2010</cite> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate [4,5].<br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in ''C. thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in ''C. acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. [1] found that ''C. thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. [1], by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. [1], by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. [1] of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2010 pmid=19345197<br /> #Warner2010a pmid=19915043<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010b Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010b. ''Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from Ruminococcus flavefaciens FD-1''. Submitted for publication.<br /> </biblio><br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5451 Glycoside Hydrolase Family 44 2010-08-15T01:05:15Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2010</cite> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate [4,5].<br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in ''C. thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. [1] found that ''C. thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. [1], by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. [1], by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. [1] of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2010 pmid=19345197<br /> #Warner2010a pmid=19915043<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010b Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010b. ''Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from Ruminococcus flavefaciens FD-1''. Submitted for publication.<br /> </biblio><br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5450 Glycoside Hydrolase Family 44 2010-08-15T01:03:02Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2010</cite> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate [4,5].<br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. [1] found that ''Clostridium thermocellum'' endoglucanase acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. [1], by testing activity of the ''C. thermocellum'' endoglucanase E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. [1], by testing activity of the ''C. thermocellum'' endoglucanase E186Q mutant.<br /> ;First 3-D structure: Kitago et al. [1] of ''C. thermocellum'' endoglucanase. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2010 pmid=19345197<br /> #Warner2010a pmid=19915043<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010b Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010b. ''Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from Ruminococcus flavefaciens FD-1''. Submitted for publication.<br /> </biblio><br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5449 Glycoside Hydrolase Family 44 2010-08-15T00:55:19Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2010</cite> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate [4,5].<br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. [1] found that the enzyme acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. [1], by testing activity of the E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. [1], by testing activity of the E186Q mutant.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2010 pmid=19345197<br /> #Warner2010a pmid=19915043<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010b Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010b. ''Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from Ruminococcus flavefaciens FD-1''. Submitted for publication.<br /> </biblio><br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5448 Glycoside Hydrolase Family 44 2010-08-15T00:53:18Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2010</cite> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate [4,5].<br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. [1] found that the enzyme acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. [1], by testing activity of the E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. [1], by testing activity of the E186Q mutant.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2010 pmid=19345197<br /> #Warner2010a pmid=19915043<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010b Warner CD, Go RM, García-Salinas C, Ford C, and Reilly PJ. 2010b. Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from ''Ruminococcus flavefaciens'' FD-1. Submitted for publication.<br /> </biblio><br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5447 Glycoside Hydrolase Family 44 2010-08-15T00:51:26Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. <cite>Kitago2007</cite> and Nam et al. <cite>Nam2010</cite> suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate [4,5].<br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. [1] found that the enzyme acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. [1], by testing activity of the E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. [1], by testing activity of the E186Q mutant.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <br /> <biblio><br /> #Kitago2007 pmid=17905739<br /> #Nam2010 pmid=19345197<br /> #Warner2010a pmid=19915043<br /> #Najmudin2006 pmid=16314409<br /> #Warner2010b Warner, CD, Go, RM, C. García-Salinas, C. Ford, and P. J. Reilly. 2010b. Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from ''Ruminococcus flavefaciens'' FD-1. Submitted for publication.<br /> </biblio><br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5422 Glycoside Hydrolase Family 44 2010-08-14T04:59:52Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. [1] and Nam et al. [2] suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be a prime substrate [4,5].<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. [1] found that the enzyme acts by a retaining mechanism. They observed that a beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. [1], by testing activity of the E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. [1], by testing activity of the E186Q mutant.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <br /> <biblio><br /> <br /> # Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44 A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> # Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> # Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010a. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> # Najmudin Najmudin, S., C. I. P. D. Guerreiro, A. L. Carvalho, J. A. M. Prates, M. A. S. Correia, V. D. Alves, L. M. A. Ferreira, M. J. Romao, H. J. Gilbert, D. N. Bolam, and C. M. G. A. Fontes. 2006. Xyloglucan Is recognized by carbohydrate-binding modules that interact with beta-glucan chains. J. Biol. Chem. 281, 8815–8828. doi: 10.1074/jbc.M510559200.<br /> # Warner Warner, C. D., R. M. Go, C. García-Salinas, C. Ford, and P. J. Reilly. 2010b. Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from ''Ruminococcus flavefaciens'' FD-1. Submitted for publication.<br /> <br /> </biblio><br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5421 Glycoside Hydrolase Family 44 2010-08-14T04:56:30Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. [1] and Nam et al. [2] suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be the prime substrate [4,5].<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. [1] found that the enzyme acts by a retaining mechanism. They observed that beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. [1], by testing activity of E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. [1], by testing activity of E186Q mutant.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <br /> <biblio><br /> <br /> # Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44 A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> # Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> # Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> # Najmudin Najmudin, S., C. I. P. D. Guerreiro, A. L. Carvalho, J. A. M. Prates, M. A. S. Correia, V. D. Alves, L. M. A. Ferreira, M. J. Romao, H. J. Gilbert, D. N. Bolam, and C. M. G. A. Fontes. 2006. Xyloglucan Is recognized by carbohydrate-binding modules that interact with beta-glucan chains. J. Biol. Chem. 281, 8815–8828. doi: 10.1074/jbc.M510559200<br /> # Warner Warner, C. D., R. M. Go, C. García-Salinas, C. Ford, and P. J. Reilly. Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from ''Ruminococcus flavefaciens'' FD-1. Submitted for publication.<br /> <br /> </biblio><br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5420 Glycoside Hydrolase Family 44 2010-08-14T04:54:23Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. [1] and Nam et al. [2] suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be the prime substrate [4,5].<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. [1] found that the enzyme acts by a retaining mechanism. They observed that beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. [1], by testing activity of E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. [1], by testing activity of E186Q mutant.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <br /> <biblio><br /> <br /> # Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44 A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> # Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> # Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> # Najmudin Najmudin, S., C. I. P. D. Guerreiro, A. L. Carvalho, J. A. M. Prates, M. A. S. Correia, V. D. Alves, L. M. A. Ferreira, M. J. Romao, H. J. Gilbert, D. N. Bolam, and C. M. G. A. Fontes. 2006. Xyloglucan Is recognized by carbohydrate-binding modules that interact with beta-glucan chains. J. Biol. Chem. 281, 8815–8828.doi: 10.1074/jbc.M510559200<br /> # Warner Warner, C. D., R. M. Go, C. García-Salinas, C. Ford, and P. J. Reilly. Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from ''Ruminococcus flavefaciens'' FD-1. Submitted for publication.<br /> <br /> </biblio><br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5419 Glycoside Hydrolase Family 44 2010-08-14T04:50:46Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. [1] and Nam et al. [2] suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be the prime substrate [4,5].<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. [1] found that the enzyme acts by a retaining mechanism. They observed that beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. [1], by testing activity of E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. [1], by testing activity of E186Q mutant.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> #Najmudin Najmudin, S., C. I. P. D. Guerreiro, A. L. Carvalho, J. A. M. Prates, M. A. S. Correia, V. D. Alves, L. M. A. Ferreira, M. J. Romao, H. J. Gilbert, D. N. Bolam, and C. M. G. A. Fontes. 2006. Xyloglucan Is recognized by carbohydrate-binding modulesthat interact with beta-glucan chains. J. Biol. Chem. 281, 8815–8828.<br /> #Warner Warner, C. D., R. M. Go, C. García-Salinas, C. Ford, and P. J. Reilly. Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from ''Ruminococcus flavefaciens'' FD-1. Submitted for publication.<br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5417 Glycoside Hydrolase Family 44 2010-08-14T03:47:19Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. [1] and Nam et al. [2] suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be the prime substrate [4,5].<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. [1] found that the enzyme acts by a retaining mechanism. They observed that beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. [1], by testing activity of E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. [1], by testing activity of E186Q mutant.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> #Najmudin Najmudin, S., C. I. Guerreiro, A. L. Carvalho, J. A. Prates, M. A. Correia, V. D. Alves, L. M. Ferreira, M. J. Romao, H. J. Gilbert, D. N. Bolam, and C. M. Fontes. 2006. J. Biol. Chem. 281, 8815–8828.<br /> #Warner Warner, C. D., R. M. Go, C. García-Salinas, C. Ford, and P. J. Reilly. Kinetic characterization of a glycoside hydrolase family 44 endoglucanase from Ruminococcus flavefaciens FD-1. Submitted for publication.<br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5416 Glycoside Hydrolase Family 44 2010-08-14T03:43:13Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. [1] and Nam et al. [2] suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be the prime substrate [4,5].<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. [1] found that the enzyme acts by a retaining mechanism. They observed that beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. [1], by testing activity of E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. [1], by testing activity of E186Q mutant.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> #Najmudin Najmudin, S., C. I. Guerreiro, A. L. Carvalho, J. A. Prates, M. A. Correia, V. D. Alves, L. M. Ferreira, M. J. Romao, H. J. Gilbert, D. N. Bolam, and C. M. Fontes. 2006. J. Biol. Chem. 281, 8815–8828.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5415 Glycoside Hydrolase Family 44 2010-08-13T21:39:56Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. [1] and Nam et al. [2] suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Active on many substances, including cellooligosaccharides of DP4 and longer, carboxymethylcellulose, xylan, lichenan, Avicel (slightly), and xyloglucan, which appears to be the prime substrate [4,5].<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. [1] found that the enzyme acts by a retaining mechanism. They observed that beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. [1], by testing activity of E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. [1], by testing activity of E186Q mutant.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> #Najmudin Najmudin, S., C. IGuerreiro, A. L. Carvalho, J. A. Prates, M. A. .Correia,,V. D..Alves, L. M.Ferreira, M. J..Romao, H. J. Gilbert, D. N. Bolam, and C. M. Fontes . 2006. J. Biol. Chem. 281, 8815–8828.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5414 Glycoside Hydrolase Family 44 2010-08-13T21:27:44Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. [1] and Nam et al. [2] suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> |Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. [1] found that the enzyme acts by a retaining mechanism. They observed that beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. [1], by testing activity of E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. [1], by testing activity of E186Q mutant.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5413 Glycoside Hydrolase Family 44 2010-08-13T21:25:44Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified, but Kitago et al. [1] and Nam et al. [2] suggest that it belongs to Clan GH-A.<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. [1] found that the enzyme acts by a retaining mechanism. They observed that beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. [1], by testing activity of E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. [1], by testing activity of E186Q mutant.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5412 Glycoside Hydrolase Family 44 2010-08-13T21:18:51Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. [1] found that the enzyme acts by a retaining mechanism. They observed that beta-anomer was preferentially formed during cyclohexaitol hydrolysis.<br /> ;First catalytic nucleophile identification: Kitago et al. [1], by testing activity of E359Q mutant.<br /> ;First general acid/base residue identification: Kitago et al. [1], by testing activity of E186Q mutant.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5411 Glycoside Hydrolase Family 44 2010-08-13T21:06:26Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Kitago et al. [1] found that the enzyme acts by a retaining mechanism. They observed that beta-anomer was preferentially formed during cyclohexinol hydrolysis.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5410 Glycoside Hydrolase Family 44 2010-08-13T21:00:49Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5409 Glycoside Hydrolase Family 44 2010-08-13T20:59:46Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 Kitago2007. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 <cite>Nam2009<cite>.''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 <cite>Warner2010<cite>.<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5408 Glycoside Hydrolase Family 44 2010-08-13T20:58:12Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 <cite>Kitago2007<cite>. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 <cite>Nam2009<cite>.''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 <cite>Warner2010<cite>.<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5407 Glycoside Hydrolase Family 44 2010-08-13T20:54:25Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase. Ca and Zn ions are found as ligands [1].<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5406 Glycoside Hydrolase Family 44 2010-08-13T20:33:16Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1], who found a TIM-like barrel domain and a beta-sandwich domain in a ''Clostridium thermocellum'' endoglucanase. Similar structures were found by Nam et al. [2] in a protein from a metagenomic library and Warner et al. [3] in a ''Clostridium acetobutylicum'' endoglucanase.<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5405 Glycoside Hydrolase Family 44 2010-08-13T20:31:24Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1] of a ''Clostridium thermocellum'' endoglucanase, who found a TIM-like barrel domain and a beta-sandwich domain. Similar structures were found by Nam et al. [2] of a protein from a metagenomic library and Warner et al. [3] of a ''Clostridium acetobutylicum'' endoglucanase.<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Kitago et al. [1] of an endoglucanase from ''Clostridium thermocellum''. It had a resolution of 0.96 Å and allowed the identification of the catalytic residues and the mechanism.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5404 Glycoside Hydrolase Family 44 2010-08-13T20:25:22Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1] of a ''Clostridium thermocellum'' endoglucanase, who found a TIM-like barrel domain and a beta-sandwich domain. Similar structures were found by Nam et al. [2] of a protein from a metagenomic library and Warner et al. [3] of a ''Clostridium acetobutylicum'' endoglucanase.<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>StickWilliams</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5403 Glycoside Hydrolase Family 44 2010-08-13T20:24:10Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359 [1]. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393 [2].''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352 [3].<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1] on a ''Clostridium thermocellum'' endoglucanase, who found a TIM-like barrel domain and a beta-sandwich domain. Similar structures were found by Nam et al. [2] on a protein from a metagenomic library and Warner et al. [3] on a ''Clostridium acetobutylicum'' endoglucanase.<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>StickWilliams</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5402 Glycoside Hydrolase Family 44 2010-08-13T20:21:59Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'' endoglucanase: catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393.''Clostridium acetobutylicum'' endoglucanase: catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352.<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1] on a ''Clostridium thermocellum'' endoglucanase, who found a TIM-like barrel domain and a beta-sandwich domain. Similar structures were found by Nam et al. [2] on a protein from a metagenomic library and Warner et al. [3] on a <br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>StickWilliams</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5401 Glycoside Hydrolase Family 44 2010-08-13T20:20:52Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum''''endoglucanase'': catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359. Protein from metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393.''Clostridium acetobutylicum''''endoglucanase'': catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352.<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1] on a ''Clostridium thermocellum'' endoglucanase, who found a TIM-like barrel domain and a beta-sandwich domain. Similar structures were found by Nam et al. [2] on a protein from a metagenomic library and Warner et al. [3] on a <br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>StickWilliams</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5400 Glycoside Hydrolase Family 44 2010-08-13T19:48:22Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'': catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359. Metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393.''Clostridium acetobutylicum'': catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352.<br /> <br /> <br /> == Three-dimensional structures ==<br /> The first three-dimensional structure was by Kitago et al. [1] on a ''Clostridium thermocellum'' endoglucanase, who found a TIM-like barrel domain and a beta-sandwich domain. Similar structures were found by Nam et al. [2] on a protein from a metagenomic library and Warner et al. [3] on a <br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>StickWilliams</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5399 Glycoside Hydrolase Family 44 2010-08-13T19:40:57Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'': catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359. Metagenomic library: catalytic proton donor/acceptor: Glu221; catalytic nucleophile: Glu393.''Clostridium acetobutylicum'': catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352.<br /> <br /> <br /> == Three-dimensional structures ==<br /> Content is to be added here.<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>StickWilliams</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from ''Clostridium thermocellum''. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from ''Clostridium acetobutylicum''. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5398 Glycoside Hydrolase Family 44 2010-08-13T19:35:55Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> Catalytic proton donor/acceptor: Glu; catalytic nucleophile: Glu<br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'': catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359. ''Clostridium acetobutylicum'': catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352<br /> <br /> <br /> == Three-dimensional structures ==<br /> Content is to be added here.<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>StickWilliams</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from Clostridium acetobutylicum. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5397 Glycoside Hydrolase Family 44 2010-08-13T19:34:06Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> <br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'': catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359. ''Clostridium acetobutylicum'': catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352<br /> <br /> <br /> == Three-dimensional structures ==<br /> Content is to be added here.<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>StickWilliams</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from Clostridium acetobutylicum. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_44&diff=5396 Glycoside Hydrolase Family 44 2010-08-13T19:33:10Z

<p>Peter Reilly: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Peter Reilly^^^<br /> * [[Responsible Curator]]: ^^^Peter Reilly^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH44'''<br /> |-<br /> |'''Clan''' <br /> |None specified<br /> |-<br /> |'''Mechanism'''<br /> |Retaining<br /> |-<br /> |'''Active site residues'''<br /> <br /> <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH44.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> ''Clostridium thermocellum'': catalytic proton donor/acceptor: Glu186; catalytic nucleophile: Glu359. ''Clostridium acetobutylicum'': catalytic proton donor/acceptor: Glu180; catalytic nucleophile: Glu352<br /> <br /> <br /> == Three-dimensional structures ==<br /> Content is to be added here.<br /> <br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>StickWilliams</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Kitago, Y., S. Karita, N. Watanabe, M. Kamiya, T. Aizawa, K. Sakka, and I. Tanaka. 2007. Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum. J. Biol. Chem. 282, 35703–35711. doi: 10.1074/jbc.M706835200.<br /> #Nam, K. H., S.-J. Kim, and K. Y. Hwang. 2009. Crystal structure of CelM2, a bifunctional glucanase–xylanase protein from a metagenomic library. Biochem. Biophys. Res. Comm. 383, 183–186. doi:10.1016/j.bbrc.2009.03.149.<br /> #Warner, C. D., J. A. Hoy, T. C. Shilling, M. J. Linnen, N. D. Ginder, C. F. Ford, R. B. Honzatko, and P. J. Reilly. 2010. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from Clostridium acetobutylicum. Appl. Environ. Microbiol., 76, 338–346. doi:10.1128/AEM.02026-09.<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH044]]</div>

Peter Reilly