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https://www.cazypedia.org/api.php?action=feedcontributions&feedformat=atom&user=Wataru+Saburi CAZypedia - User contributions [en-ca] 2026-05-05T02:03:25Z User contributions MediaWiki 1.35.10 https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=12494 Glycoside Hydrolase Family 130 2018-02-16T02:40:16Z

<p>Wataru Saburi: /* References */</p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |none<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Family [[GH130]] contains [[phosphorylases]] and a hydrolase acting on &beta;-mannosides. This family was created based on the identification of 4-''O''-&beta;-D-mannosyl-D-glucose phosphorylase activity (EC [{{EClink}}2.4.1.281 2.4.1.281]) for the protein (BfMGP) derived from the gene BF0772 of ''Bacteroides fragilis'' <cite>Senoura2011</cite>. This enzyme is likely involved in the degradation of &beta;-1,4-mannobiose together with cellobiose 2-epimerase, which converts &beta;-1,4-mannobiose to 4-''O''-&beta;-D-mannosyl-D-glucose. Other activities within the family include: &beta;-1,4-mannooligosaccharide phosphorylase (EC [{{EClink}}2.4.1.319 2.4.1.319]) <cite>Kawahara2012</cite>, 1,4-&beta;-mannosyl-''N''-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) <cite>Nihira2013</cite> <cite>Ladeveze2013</cite>, 1,2-&beta;-oligomannan phosphorylase <cite>Chiku2014</cite>, &beta;-1,2-mannnobiose phosphorylase <cite>Chiku2014</cite>, and &beta;-1,2-mannosidase <cite>Cuskin2015</cite> <cite>Nihira2015</cite><br /> <br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;-mannosidic linkages at the non-reducing end of substrates with net [[inverting|inversion]] of anomeric configuration affording &alpha;-mannose-1-phosphate. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-''O''-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-''O''-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique proton relay mechanism for GH130 enzymes was proposed on the basis of the three-dimensional strucuture of BfMGP <cite>Nakae2013</cite>. In contrast to other inverting glycoside phosphorylases, where a general acid catalyst is proposed to directly protonate the glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bound to subsite -1, and a proton is transferred intramolecularly to the glycosidic oxygen from 3OH group. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated. &beta;-1,2-Mannosidase lacks some basic amino acid residues responsible for binding to inorganic phosphate in phosphorylases, but has two Glu residues acting as general base catalyst <cite>Cuskin2015</cite> <cite>Nihira2015</cite>. These residues could activate catalytic water to facilitate nucleophilic attack to the anomeric carbon of the mannosyl residue.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Mutation of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation completely abolished the catalytic activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the glycosidic oxygen <cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the glycosidic oxygen for direct protonation, and the proton relay mechanism described above was therefore proposed. In &beta;-1,2-mannosidase from ''Dyadobacter fermentans'', Glu224 and Glu265 act as general base catalyst <cite>Nihira2015</cite> to activate catalytic water.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensional structures of several GH130 phosphorylases have been reported. The structure of ''Bacteroides fragilis'' BfMGP has been reported in complex with phosphate; 4-''O''-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate <cite>Nakae2013</cite>. BfMGP forms a homohexamer, and each monomer has a five-bladed &beta;-propeller fold. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: ''Bacteroides fragilis'' BfMGP <cite>Senoura2011</cite><br /> ;First general acid residue identification: ''Bacteroides fragilis'' BfMGP <cite>Nakae2013</cite><br /> ;First 3-D structure: ''Bacteroides fragilis'' BfMGP <cite>Nakae2013</cite><br /> <br /> == References ==<br /> <biblio><br /> #Ladeveze2013 pmid=24043624<br /> <br /> #Senoura2011 pmid=21539815<br /> <br /> #Nakae2013 pmid=23954514<br /> <br /> #Kawahara2012 pmid=23093406<br /> <br /> #Nihira2013 pmid=23943617<br /> <br /> #Cuskin2015 pmid=26286752<br /> <br /> #Nihira2015 pmid=26476324 <br /> <br /> <br /> #Chiku2014 pmid=25500577<br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=12493 Glycoside Hydrolase Family 130 2018-02-16T02:35:51Z

<p>Wataru Saburi: /* Catalytic Residues */</p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |none<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Family [[GH130]] contains [[phosphorylases]] and a hydrolase acting on &beta;-mannosides. This family was created based on the identification of 4-''O''-&beta;-D-mannosyl-D-glucose phosphorylase activity (EC [{{EClink}}2.4.1.281 2.4.1.281]) for the protein (BfMGP) derived from the gene BF0772 of ''Bacteroides fragilis'' <cite>Senoura2011</cite>. This enzyme is likely involved in the degradation of &beta;-1,4-mannobiose together with cellobiose 2-epimerase, which converts &beta;-1,4-mannobiose to 4-''O''-&beta;-D-mannosyl-D-glucose. Other activities within the family include: &beta;-1,4-mannooligosaccharide phosphorylase (EC [{{EClink}}2.4.1.319 2.4.1.319]) <cite>Kawahara2012</cite>, 1,4-&beta;-mannosyl-''N''-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) <cite>Nihira2013</cite> <cite>Ladeveze2013</cite>, 1,2-&beta;-oligomannan phosphorylase <cite>Chiku2014</cite>, &beta;-1,2-mannnobiose phosphorylase <cite>Chiku2014</cite>, and &beta;-1,2-mannosidase <cite>Cuskin2015</cite> <cite>Nihira2015</cite><br /> <br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;-mannosidic linkages at the non-reducing end of substrates with net [[inverting|inversion]] of anomeric configuration affording &alpha;-mannose-1-phosphate. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-''O''-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-''O''-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique proton relay mechanism for GH130 enzymes was proposed on the basis of the three-dimensional strucuture of BfMGP <cite>Nakae2013</cite>. In contrast to other inverting glycoside phosphorylases, where a general acid catalyst is proposed to directly protonate the glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bound to subsite -1, and a proton is transferred intramolecularly to the glycosidic oxygen from 3OH group. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated. &beta;-1,2-Mannosidase lacks some basic amino acid residues responsible for binding to inorganic phosphate in phosphorylases, but has two Glu residues acting as general base catalyst <cite>Cuskin2015</cite> <cite>Nihira2015</cite>. These residues could activate catalytic water to facilitate nucleophilic attack to the anomeric carbon of the mannosyl residue.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Mutation of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation completely abolished the catalytic activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the glycosidic oxygen <cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the glycosidic oxygen for direct protonation, and the proton relay mechanism described above was therefore proposed. In &beta;-1,2-mannosidase from ''Dyadobacter fermentans'', Glu224 and Glu265 act as general base catalyst <cite>Nihira2015</cite> to activate catalytic water.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensional structures of several GH130 phosphorylases have been reported. The structure of ''Bacteroides fragilis'' BfMGP has been reported in complex with phosphate; 4-''O''-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate <cite>Nakae2013</cite>. BfMGP forms a homohexamer, and each monomer has a five-bladed &beta;-propeller fold. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: ''Bacteroides fragilis'' BfMGP <cite>Senoura2011</cite><br /> ;First general acid residue identification: ''Bacteroides fragilis'' BfMGP <cite>Nakae2013</cite><br /> ;First 3-D structure: ''Bacteroides fragilis'' BfMGP <cite>Nakae2013</cite><br /> <br /> == References ==<br /> <biblio><br /> #Ladeveze2013 pmid=24043624<br /> <br /> #Senoura2011 pmid=21539815<br /> <br /> #Nakae2013 pmid=23954514<br /> <br /> #Kawahara2012 pmid=23093406<br /> <br /> #Nihira2013 pmid=23943617<br /> #Chiku2014 pmid=25500577<br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=12492 Glycoside Hydrolase Family 130 2018-02-16T02:34:40Z

<p>Wataru Saburi: /* Catalytic Residues */</p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |none<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Family [[GH130]] contains [[phosphorylases]] and a hydrolase acting on &beta;-mannosides. This family was created based on the identification of 4-''O''-&beta;-D-mannosyl-D-glucose phosphorylase activity (EC [{{EClink}}2.4.1.281 2.4.1.281]) for the protein (BfMGP) derived from the gene BF0772 of ''Bacteroides fragilis'' <cite>Senoura2011</cite>. This enzyme is likely involved in the degradation of &beta;-1,4-mannobiose together with cellobiose 2-epimerase, which converts &beta;-1,4-mannobiose to 4-''O''-&beta;-D-mannosyl-D-glucose. Other activities within the family include: &beta;-1,4-mannooligosaccharide phosphorylase (EC [{{EClink}}2.4.1.319 2.4.1.319]) <cite>Kawahara2012</cite>, 1,4-&beta;-mannosyl-''N''-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) <cite>Nihira2013</cite> <cite>Ladeveze2013</cite>, 1,2-&beta;-oligomannan phosphorylase <cite>Chiku2014</cite>, &beta;-1,2-mannnobiose phosphorylase <cite>Chiku2014</cite>, and &beta;-1,2-mannosidase <cite>Cuskin2015</cite> <cite>Nihira2015</cite><br /> <br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;-mannosidic linkages at the non-reducing end of substrates with net [[inverting|inversion]] of anomeric configuration affording &alpha;-mannose-1-phosphate. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-''O''-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-''O''-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique proton relay mechanism for GH130 enzymes was proposed on the basis of the three-dimensional strucuture of BfMGP <cite>Nakae2013</cite>. In contrast to other inverting glycoside phosphorylases, where a general acid catalyst is proposed to directly protonate the glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bound to subsite -1, and a proton is transferred intramolecularly to the glycosidic oxygen from 3OH group. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated. &beta;-1,2-Mannosidase lacks some basic amino acid residues responsible for binding to inorganic phosphate in phosphorylases, but has two Glu residues acting as general base catalyst <cite>Cuskin2015</cite> <cite>Nihira2015</cite>. These residues could activate catalytic water to facilitate nucleophilic attack to the anomeric carbon of the mannosyl residue.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Mutation of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation completely abolished the catalytic activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the glycosidic oxygen <cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the glycosidic oxygen for direct protonation, and the proton relay mechanism described above was therefore proposed. In &beta;-1,2-Mannosidase from Dyadobacter fermentans, Glu224 and Glu265 act as general base catalyst <cite>Nihira2015</cite> to activate catalytic water.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensional structures of several GH130 phosphorylases have been reported. The structure of ''Bacteroides fragilis'' BfMGP has been reported in complex with phosphate; 4-''O''-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate <cite>Nakae2013</cite>. BfMGP forms a homohexamer, and each monomer has a five-bladed &beta;-propeller fold. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: ''Bacteroides fragilis'' BfMGP <cite>Senoura2011</cite><br /> ;First general acid residue identification: ''Bacteroides fragilis'' BfMGP <cite>Nakae2013</cite><br /> ;First 3-D structure: ''Bacteroides fragilis'' BfMGP <cite>Nakae2013</cite><br /> <br /> == References ==<br /> <biblio><br /> #Ladeveze2013 pmid=24043624<br /> <br /> #Senoura2011 pmid=21539815<br /> <br /> #Nakae2013 pmid=23954514<br /> <br /> #Kawahara2012 pmid=23093406<br /> <br /> #Nihira2013 pmid=23943617<br /> #Chiku2014 pmid=25500577<br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=12491 Glycoside Hydrolase Family 130 2018-02-16T02:29:39Z

<p>Wataru Saburi: /* Kinetics and Mechanism */</p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |none<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Family [[GH130]] contains [[phosphorylases]] and a hydrolase acting on &beta;-mannosides. This family was created based on the identification of 4-''O''-&beta;-D-mannosyl-D-glucose phosphorylase activity (EC [{{EClink}}2.4.1.281 2.4.1.281]) for the protein (BfMGP) derived from the gene BF0772 of ''Bacteroides fragilis'' <cite>Senoura2011</cite>. This enzyme is likely involved in the degradation of &beta;-1,4-mannobiose together with cellobiose 2-epimerase, which converts &beta;-1,4-mannobiose to 4-''O''-&beta;-D-mannosyl-D-glucose. Other activities within the family include: &beta;-1,4-mannooligosaccharide phosphorylase (EC [{{EClink}}2.4.1.319 2.4.1.319]) <cite>Kawahara2012</cite>, 1,4-&beta;-mannosyl-''N''-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) <cite>Nihira2013</cite> <cite>Ladeveze2013</cite>, 1,2-&beta;-oligomannan phosphorylase <cite>Chiku2014</cite>, &beta;-1,2-mannnobiose phosphorylase <cite>Chiku2014</cite>, and &beta;-1,2-mannosidase <cite>Cuskin2015</cite> <cite>Nihira2015</cite><br /> <br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;-mannosidic linkages at the non-reducing end of substrates with net [[inverting|inversion]] of anomeric configuration affording &alpha;-mannose-1-phosphate. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-''O''-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-''O''-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique proton relay mechanism for GH130 enzymes was proposed on the basis of the three-dimensional strucuture of BfMGP <cite>Nakae2013</cite>. In contrast to other inverting glycoside phosphorylases, where a general acid catalyst is proposed to directly protonate the glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bound to subsite -1, and a proton is transferred intramolecularly to the glycosidic oxygen from 3OH group. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated. &beta;-1,2-Mannosidase lacks some basic amino acid residues responsible for binding to inorganic phosphate in phosphorylases, but has two Glu residues acting as general base catalyst <cite>Cuskin2015</cite> <cite>Nihira2015</cite>. These residues could activate catalytic water to facilitate nucleophilic attack to the anomeric carbon of the mannosyl residue.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Mutation of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation completely abolished the catalytic activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the glycosidic oxygen <cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the glycosidic oxygen for direct protonation, and the proton relay mechanism described above was therefore proposed.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensional structures of several GH130 phosphorylases have been reported. The structure of ''Bacteroides fragilis'' BfMGP has been reported in complex with phosphate; 4-''O''-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate <cite>Nakae2013</cite>. BfMGP forms a homohexamer, and each monomer has a five-bladed &beta;-propeller fold. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: ''Bacteroides fragilis'' BfMGP <cite>Senoura2011</cite><br /> ;First general acid residue identification: ''Bacteroides fragilis'' BfMGP <cite>Nakae2013</cite><br /> ;First 3-D structure: ''Bacteroides fragilis'' BfMGP <cite>Nakae2013</cite><br /> <br /> == References ==<br /> <biblio><br /> #Ladeveze2013 pmid=24043624<br /> <br /> #Senoura2011 pmid=21539815<br /> <br /> #Nakae2013 pmid=23954514<br /> <br /> #Kawahara2012 pmid=23093406<br /> <br /> #Nihira2013 pmid=23943617<br /> #Chiku2014 pmid=25500577<br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=12490 Glycoside Hydrolase Family 130 2018-02-16T02:28:05Z

<p>Wataru Saburi: /* Kinetics and Mechanism */</p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |none<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Family [[GH130]] contains [[phosphorylases]] and a hydrolase acting on &beta;-mannosides. This family was created based on the identification of 4-''O''-&beta;-D-mannosyl-D-glucose phosphorylase activity (EC [{{EClink}}2.4.1.281 2.4.1.281]) for the protein (BfMGP) derived from the gene BF0772 of ''Bacteroides fragilis'' <cite>Senoura2011</cite>. This enzyme is likely involved in the degradation of &beta;-1,4-mannobiose together with cellobiose 2-epimerase, which converts &beta;-1,4-mannobiose to 4-''O''-&beta;-D-mannosyl-D-glucose. Other activities within the family include: &beta;-1,4-mannooligosaccharide phosphorylase (EC [{{EClink}}2.4.1.319 2.4.1.319]) <cite>Kawahara2012</cite>, 1,4-&beta;-mannosyl-''N''-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) <cite>Nihira2013</cite> <cite>Ladeveze2013</cite>, 1,2-&beta;-oligomannan phosphorylase <cite>Chiku2014</cite>, &beta;-1,2-mannnobiose phosphorylase <cite>Chiku2014</cite>, and &beta;-1,2-mannosidase <cite>Cuskin2015</cite> <cite>Nihira2015</cite><br /> <br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;-mannosidic linkages at the non-reducing end of substrates with net [[inverting|inversion]] of anomeric configuration affording &alpha;-mannose-1-phosphate. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-''O''-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-''O''-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique proton relay mechanism for GH130 enzymes was proposed on the basis of the three-dimensional strucuture of BfMGP <cite>Nakae2013</cite>. In contrast to other inverting glycoside phosphorylases, where a general acid catalyst is proposed to directly protonate the glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bound to subsite -1, and a proton is transferred intramolecularly to the glycosidic oxygen from 3OH group. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated. &beta;-1,2-Mannosidase lacks some basic amino acid residues responsible for binding to inorganic phosphate in phosphorylases, but has two Glu residues acting as general base catalyst.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Mutation of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation completely abolished the catalytic activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the glycosidic oxygen <cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the glycosidic oxygen for direct protonation, and the proton relay mechanism described above was therefore proposed.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensional structures of several GH130 phosphorylases have been reported. The structure of ''Bacteroides fragilis'' BfMGP has been reported in complex with phosphate; 4-''O''-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate <cite>Nakae2013</cite>. BfMGP forms a homohexamer, and each monomer has a five-bladed &beta;-propeller fold. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: ''Bacteroides fragilis'' BfMGP <cite>Senoura2011</cite><br /> ;First general acid residue identification: ''Bacteroides fragilis'' BfMGP <cite>Nakae2013</cite><br /> ;First 3-D structure: ''Bacteroides fragilis'' BfMGP <cite>Nakae2013</cite><br /> <br /> == References ==<br /> <biblio><br /> #Ladeveze2013 pmid=24043624<br /> <br /> #Senoura2011 pmid=21539815<br /> <br /> #Nakae2013 pmid=23954514<br /> <br /> #Kawahara2012 pmid=23093406<br /> <br /> #Nihira2013 pmid=23943617<br /> #Chiku2014 pmid=25500577<br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=12489 Glycoside Hydrolase Family 130 2018-02-16T02:21:35Z

<p>Wataru Saburi: /* Substrate specificities */</p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |none<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Family [[GH130]] contains [[phosphorylases]] and a hydrolase acting on &beta;-mannosides. This family was created based on the identification of 4-''O''-&beta;-D-mannosyl-D-glucose phosphorylase activity (EC [{{EClink}}2.4.1.281 2.4.1.281]) for the protein (BfMGP) derived from the gene BF0772 of ''Bacteroides fragilis'' <cite>Senoura2011</cite>. This enzyme is likely involved in the degradation of &beta;-1,4-mannobiose together with cellobiose 2-epimerase, which converts &beta;-1,4-mannobiose to 4-''O''-&beta;-D-mannosyl-D-glucose. Other activities within the family include: &beta;-1,4-mannooligosaccharide phosphorylase (EC [{{EClink}}2.4.1.319 2.4.1.319]) <cite>Kawahara2012</cite>, 1,4-&beta;-mannosyl-''N''-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) <cite>Nihira2013</cite> <cite>Ladeveze2013</cite>, 1,2-&beta;-oligomannan phosphorylase <cite>Chiku2014</cite>, &beta;-1,2-mannnobiose phosphorylase <cite>Chiku2014</cite>, and &beta;-1,2-mannosidase <cite>Cuskin2015</cite> <cite>Nihira2015</cite><br /> <br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;-mannosidic linkages at the non-reducing end of substrates with net [[inverting|inversion]] of anomeric configuration affording &alpha;-mannose-1-phosphate. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-''O''-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-''O''-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique proton relay mechanism for GH130 enzymes was proposed on the basis of the three-dimensional strucuture of BfMGP <cite>Nakae2013</cite>. In contrast to other inverting glycoside phosphorylases, where a general acid catalyst is proposed to directly protonate the glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bound to subsite -1, and a proton is transferred intramolecularly to the glycosidic oxygen from 3OH group. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Mutation of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation completely abolished the catalytic activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the glycosidic oxygen <cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the glycosidic oxygen for direct protonation, and the proton relay mechanism described above was therefore proposed.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensional structures of several GH130 phosphorylases have been reported. The structure of ''Bacteroides fragilis'' BfMGP has been reported in complex with phosphate; 4-''O''-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate <cite>Nakae2013</cite>. BfMGP forms a homohexamer, and each monomer has a five-bladed &beta;-propeller fold. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: ''Bacteroides fragilis'' BfMGP <cite>Senoura2011</cite><br /> ;First general acid residue identification: ''Bacteroides fragilis'' BfMGP <cite>Nakae2013</cite><br /> ;First 3-D structure: ''Bacteroides fragilis'' BfMGP <cite>Nakae2013</cite><br /> <br /> == References ==<br /> <biblio><br /> #Ladeveze2013 pmid=24043624<br /> <br /> #Senoura2011 pmid=21539815<br /> <br /> #Nakae2013 pmid=23954514<br /> <br /> #Kawahara2012 pmid=23093406<br /> <br /> #Nihira2013 pmid=23943617<br /> #Chiku2014 pmid=25500577<br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=12488 Glycoside Hydrolase Family 130 2018-02-16T02:20:14Z

<p>Wataru Saburi: /* Substrate specificities */</p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |none<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Family [[GH130]] contains [[phosphorylases]] and a hydrolase acting on &beta;-mannosides. This family was created based on the identification of 4-''O''-&beta;-D-mannosyl-D-glucose phosphorylase activity (EC [{{EClink}}2.4.1.281 2.4.1.281]) for the protein (BfMGP) derived from the gene BF0772 of ''Bacteroides fragilis'' <cite>Senoura2011</cite>. This enzyme is likely involved in degradation of &beta;-1,4-D-mannobiose together with cellobiose 2-epimerase, which converts &beta;-1,4-D-mannobiose to 4-''O''-&beta;-D-mannosyl-D-glucose. Other activities within the family include: &beta;-1,4-mannooligosaccharide phosphorylase (EC [{{EClink}}2.4.1.319 2.4.1.319]) <cite>Kawahara2012</cite>, 1,4-&beta;-mannosyl-''N''-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) <cite>Nihira2013</cite> <cite>Ladeveze2013</cite>, 1,2-&beta;-oligomannan phosphorylase <cite>Chiku2014</cite>, &beta;-1,2-mannnobiose phosphorylase <cite>Chiku2014</cite>, and &beta;-1,2-mannosidase <cite>Cuskin2015</cite> <cite>Nihira2015</cite><br /> <br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;-mannosidic linkages at the non-reducing end of substrates with net [[inverting|inversion]] of anomeric configuration affording &alpha;-mannose-1-phosphate. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-''O''-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-''O''-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique proton relay mechanism for GH130 enzymes was proposed on the basis of the three-dimensional strucuture of BfMGP <cite>Nakae2013</cite>. In contrast to other inverting glycoside phosphorylases, where a general acid catalyst is proposed to directly protonate the glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bound to subsite -1, and a proton is transferred intramolecularly to the glycosidic oxygen from 3OH group. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Mutation of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation completely abolished the catalytic activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the glycosidic oxygen <cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the glycosidic oxygen for direct protonation, and the proton relay mechanism described above was therefore proposed.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensional structures of several GH130 phosphorylases have been reported. The structure of ''Bacteroides fragilis'' BfMGP has been reported in complex with phosphate; 4-''O''-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate <cite>Nakae2013</cite>. BfMGP forms a homohexamer, and each monomer has a five-bladed &beta;-propeller fold. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: ''Bacteroides fragilis'' BfMGP <cite>Senoura2011</cite><br /> ;First general acid residue identification: ''Bacteroides fragilis'' BfMGP <cite>Nakae2013</cite><br /> ;First 3-D structure: ''Bacteroides fragilis'' BfMGP <cite>Nakae2013</cite><br /> <br /> == References ==<br /> <biblio><br /> #Ladeveze2013 pmid=24043624<br /> <br /> #Senoura2011 pmid=21539815<br /> <br /> #Nakae2013 pmid=23954514<br /> <br /> #Kawahara2012 pmid=23093406<br /> <br /> #Nihira2013 pmid=23943617<br /> #Chiku2014 pmid=25500577<br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=User:Wataru_Saburi&diff=10569 User:Wataru Saburi 2015-03-17T06:44:03Z

<p>Wataru Saburi: </p> <hr /> <div>[[<br /> <br /> Image:Saburi2.jpg|200px|right]]<br /> <br /> '''Wataru Saburi''' is an assistant professor at Laboratory of Biochemistry in Research Faculty of Agriculture, Hokkaido University (Sapporo, Japan). He obtained Ph. D from Graduate School of Agriculture, Hokkaido University in 2006, under the supervision of Professor Atsuo Kimura. He joined the Research Institute of Nihon Shokuhin Kako Co. Ltd. as a researcher (2006-2010), and developed functional oligosaccharides produced from starch. His research interests are structures and functions of carbohydrate active enzymes and efficient synthesis of functional oligosaccharides. He has studied about<br /> <br /> * [[GH1]] rice β-glucosidase <cite>Himeno2013</cite><br /> * [[GH13]] ''Bacillus'' sp. AAH-31 α-amylase <cite>Kim2012 Saburia2013</cite><br /> * [[GH13]] ''Streptococcus mutans'' dextran glucosidase <cite>Saburi2006 Saburi2007 Hondoh2008 Kobayashi2011 Saburib2013 Saburi2015b Kobayashi2015</cite><br /> * [[GH13]] ''Halomonas'' sp. H11 α-glucosidase <cite>Ojima2012</cite><br /> * [[GH13]] ''Bacillus clarkii'' γ-cyclodextrinase <cite>Nakagawa2008</cite><br /> * [[GH31]] ''Bacillus'' sp. AHU 2001 α-glucosidase BspAG31A <cite>Saburi2014</cite><br /> * [[GH94]] ''Ruminococcus albus'' cellobiose phosphorylase <cite>Hamura2012 Hamura2013</cite><br /> * [[GH94]] ''Ruminococcus albus'' cellodextrin phosphorylase <cite>Sawano2013</cite><br /> * [[GH130]] ''Ruminococcus albus'' 4-''O''-β-mannosylglucose phosphorylase (RaMP1) <cite>Kawahara2012</cite><br /> * [[GH130]] ''Rhodothermus marinus'' 4-''O''-β-mannosylglucose phosphorylase <cite>Jaito2014</cite><br /> <br /> * [[GH130]] ''Cellvibrio vulgaris'' 4-''O''-β-mannosylglucose phosphorylase <cite>Saburi2015</cite><br /> * [[GH130]] ''Ruminococcus albus'' β-1,4-mannooligosaccharide phosphorylase (RaMP2) <cite>Kawahara2012</cite><br /> <br /> <br /> <br /> ----<br /> <br /> <biblio><br /> #Himeno2013 pmid=23649259<br /> #>Kim2012 pmid=22785486<br /> #>Saburia2013 pmid=24018662<br /> #>Saburi2006 pmid=16503208<br /> #>Saburi2007 pmid=17768352<br /> #>Hondoh2008 pmid=18395742<br /> #>Kobayashi2011 pmid=21821929<br /> #>Saburib2013 pmid=24052257<br /> #>Ojima2012 pmid=22226947<br /> #>Nakagawa2008 pmid=18824139<br /> #>Saburi2014 pmid=25450253<br /> #>Hamura2012 pmid=22484959<br /> #>Hamura2013 pmid=23845516<br /> #>Sawano2013 pmid=23802549<br /> #>Kawahara2012 pmid=23093406<br /> #>Jaito2014 pmid=25036679<br /> <br /> #>Saburi2015 pmid=25704402<br /> <br /> #>Saburi2015b pmid=25728274<br /> <br /> #>Kobayashi2015 pmid=25595454<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Contributors|Saburi,Wataru]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=User:Wataru_Saburi&diff=10568 User:Wataru Saburi 2015-03-17T06:42:27Z

<p>Wataru Saburi: </p> <hr /> <div>[[<br /> <br /> Image:Saburi2.jpg|200px|right]]<br /> <br /> '''Wataru Saburi''' is an assistant professor at Laboratory of Biochemistry in Research Faculty of Agriculture, Hokkaido University (Sapporo, Japan). He obtained Ph. D from Graduate School of Agriculture, Hokkaido University in 2006, under the supervision of Professor Atsuo Kimura. He joined the Research Institute of Nihon Shokuhin Kako Co. Ltd. as a researcher (2006-2010), and developed functional oligosaccharides produced from starch. His research interests are structures and functions of carbohydrate active enzymes and efficient synthesis of functional oligosaccharides. He has studied about<br /> <br /> * [[GH1]] rice β-glucosidase <cite>Himeno2013</cite><br /> * [[GH13]] ''Bacillus'' sp. AAH-31 α-amylase <cite>Kim2012 Saburia2013</cite><br /> * [[GH13]] Streptococcus mutans dextran glucosidase <cite>Saburi2006 Saburi2007 Hondoh2008 Kobayashi2011 Saburib2013 Saburi2015b Kobayashi2015</cite><br /> * [[GH13]] Halomonas sp. H11 α-glucosidase <cite>Ojima2012</cite><br /> * [[GH13]] Bacillus clarkii γ-cyclodextrinase <cite>Nakagawa2008</cite><br /> * [[GH31]] Bacillus sp. AHU 2001 α-glucosidase BspAG31A <cite>Saburi2014</cite><br /> * [[GH94]] Ruminococcus albus cellobiose phosphorylase <cite>Hamura2012 Hamura2013</cite><br /> * [[GH94]] Ruminococcus albus cellodextrin phosphorylase <cite>Sawano2013</cite><br /> * [[GH130]] Ruminococcus albus 4-O-β-mannosylglucose phosphorylase (RaMP1) <cite>Kawahara2012</cite><br /> * [[GH130]] Rhodothermus marinus 4-O-β-mannosylglucose phosphorylase <cite>Jaito2014</cite><br /> <br /> * [[GH130]] Cellvibrio vulgaris 4-O-β-mannosylglucose phosphorylase <cite>Saburi2015</cite><br /> * [[GH130]] Ruminococcus albus β-1,4-mannooligosaccharide phosphorylase (RaMP2) <cite>Kawahara2012</cite><br /> <br /> <br /> <br /> ----<br /> <br /> <biblio><br /> #Himeno2013 pmid=23649259<br /> #>Kim2012 pmid=22785486<br /> #>Saburia2013 pmid=24018662<br /> #>Saburi2006 pmid=16503208<br /> #>Saburi2007 pmid=17768352<br /> #>Hondoh2008 pmid=18395742<br /> #>Kobayashi2011 pmid=21821929<br /> #>Saburib2013 pmid=24052257<br /> #>Ojima2012 pmid=22226947<br /> #>Nakagawa2008 pmid=18824139<br /> #>Saburi2014 pmid=25450253<br /> #>Hamura2012 pmid=22484959<br /> #>Hamura2013 pmid=23845516<br /> #>Sawano2013 pmid=23802549<br /> #>Kawahara2012 pmid=23093406<br /> #>Jaito2014 pmid=25036679<br /> <br /> #>Saburi2015 pmid=25704402<br /> <br /> #>Saburi2015b pmid=25728274<br /> <br /> #>Kobayashi2015 pmid=25595454<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Contributors|Saburi,Wataru]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=User:Wataru_Saburi&diff=10567 User:Wataru Saburi 2015-03-17T06:35:58Z

<p>Wataru Saburi: </p> <hr /> <div>[[<br /> <br /> Image:Saburi2.jpg|200px|right]]<br /> <br /> '''Wataru Saburi''' is an assistant professor at Laboratory of Biochemistry in Research Faculty of Agriculture, Hokkaido University (Sapporo, Japan). He obtained Ph. D from Graduate School of Agriculture, Hokkaido University in 2006, under the supervision of Professor Atsuo Kimura. He joined the Research Institute of Nihon Shokuhin Kako Co. Ltd. as a researcher (2006-2010), and developed functional oligosaccharides produced from starch. His research interests are structures and functions of carbohydrate active enzymes and efficient synthesis of functional oligosaccharides. He has studied about<br /> <br /> * [[GH1]] rice β-glucosidase <cite>Himeno2013</cite><br /> * [[GH13]] Bacillus sp. AAH-31 α-amylase <cite>Kim2012 Saburia2013</cite><br /> * [[GH13]] Streptococcus mutans dextran glucosidase <cite>Saburi2006 Saburi2007 Hondoh2008 Kobayashi2011 Saburib2013 Saburi2015b Kobayashi2015</cite><br /> * [[GH13]] Halomonas sp. H11 α-glucosidase <cite>Ojima2012</cite><br /> * [[GH13]] Bacillus clarkii γ-cyclodextrinase <cite>Nakagawa2008</cite><br /> * [[GH31]] Bacillus sp. AHU 2001 α-glucosidase BspAG31A <cite>Saburi2014</cite><br /> * [[GH94]] Ruminococcus albus cellobiose phosphorylase <cite>Hamura2012 Hamura2013</cite><br /> * [[GH94]] Ruminococcus albus cellodextrin phosphorylase <cite>Sawano2013</cite><br /> * [[GH130]] Ruminococcus albus 4-O-β-mannosylglucose phosphorylase (RaMP1) <cite>Kawahara2012</cite><br /> * [[GH130]] Rhodothermus marinus 4-O-β-mannosylglucose phosphorylase <cite>Jaito2014</cite><br /> <br /> * [[GH130]] Cellvibrio vulgaris 4-O-β-mannosylglucose phosphorylase <cite>Saburi2015</cite><br /> * [[GH130]] Ruminococcus albus β-1,4-mannooligosaccharide phosphorylase (RaMP2) <cite>Kawahara2012</cite><br /> <br /> <br /> <br /> ----<br /> <br /> <biblio><br /> #Himeno2013 pmid=23649259<br /> #>Kim2012 pmid=22785486<br /> #>Saburia2013 pmid=24018662<br /> #>Saburi2006 pmid=16503208<br /> #>Saburi2007 pmid=17768352<br /> #>Hondoh2008 pmid=18395742<br /> #>Kobayashi2011 pmid=21821929<br /> #>Saburib2013 pmid=24052257<br /> #>Ojima2012 pmid=22226947<br /> #>Nakagawa2008 pmid=18824139<br /> #>Saburi2014 pmid=25450253<br /> #>Hamura2012 pmid=22484959<br /> #>Hamura2013 pmid=23845516<br /> #>Sawano2013 pmid=23802549<br /> #>Kawahara2012 pmid=23093406<br /> #>Jaito2014 pmid=25036679<br /> <br /> #>Saburi2015 pmid=25704402<br /> <br /> #>Saburi2015b pmid=25728274<br /> <br /> #>Kobayashi2015 pmid=25595454<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Contributors|Saburi,Wataru]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10566 Glycoside Hydrolase Family 130 2015-03-17T04:05:31Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |none<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;-mannosidic linkage at the non-reducing end of substrates. 4-''O''-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase (EC [{{EClink}}2.4.1.319 2.4.1.319]), 1,4-&beta;-mannosyl-''N''-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]), 1,2-&beta;-oligomannan phosphorylase, and &beta;-1,2-mannnobiose phosphorylase are members of this family. A GH130 mannoside phosphorylase, unknown human gut bacterium mannoside phosphorylase (UhgbMP), discovered by functional metagenomics of the human gut microbiota, phosphorolyzes 4-''O''-&beta;-D-mannosyl-N,N'-diacetylchitobiose, and exhibits higher synthetic activity to ''N'',''N'''-diacetylchitobiose as an acceptor substrate than ''N''-acetyl-D-glucosamine <cite>Ladeveze2013</cite>.<br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;-mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-''O''-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-''O''-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture of BfMGP <cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bound to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Substitution of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation comletely abolished the activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the scicile glycosidic oxigen <cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the scicile glycosidic oxigen for a direct protonation. Thus the proton relay mechanism described above has been posturated.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensinal structure of BfMGP has been first reported as a characterized enzyme <cite>Nakae2013</cite>. The structures of BfMGP in complex with phosphate; 4-''O''-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate were determined. The structure of catalytic domain of BfMGP is a five-bladed &beta;-propeller fold. BfMGP forms a homohexamer. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: BfMGP <cite>Senoura2011</cite><br /> ;First general acid residue identification: BfMGP <cite>Nakae2013</cite><br /> ;First sequence identification: BfMGP <cite>Senoura2011</cite><br /> <br /> : Ruminococcus albus &beta;-1,4-mannooligosaccharide phosphorylase <cite>Kawahara2012</cite><br /> <br /> : Bacteroides thetaiotaomicron 4-''O''-&beta;-D-Mannosyl-D-glucose phosphorylase <cite>Nihira2013</cite> <br /> <br /> : Thermoanaerobacter sp. X-514 1,2-&beta;-oligomannan phosphorylase <cite>Chiku2014</cite> <br /> <br /> : Thermoanaerobacter sp. X-514 &beta;-1,2-mannnobiose phosphorylase <cite>Chiku2014</cite> <br /> <br /> ;First 3-D structure: BfMGP <cite>Nakae2013</cite><br /> <br /> == References ==<br /> <biblio><br /> #Ladeveze2013 pmid=24043624<br /> <br /> #Senoura2011 pmid=21539815<br /> <br /> #Nakae2013 pmid=23954514<br /> <br /> #Kawahara2012 pmid=23093406<br /> <br /> #Nihira2013 pmid=23943617<br /> #Chiku2014 pmid=25500577<br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10513 Glycoside Hydrolase Family 130 2015-02-12T00:54:24Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;-mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase (EC [{{EClink}}2.4.1.319 2.4.1.319]), 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]), 1,2-&beta;-oligomannan phosphorylase, and &beta;-1,2-mannnobiose phosphorylase are members of this family. A GH130 mannoside phosphorylase, unknown human gut bacterium mannoside phosphorylase (UhgbMP), discovered by functional metagenomics of the human gut microbiota, phosphorolyzes 4-O-&beta;-D-mannosyl-N,N'-diacetylchitobiose, and exhibits higher synthetic activity to N,N'-diacetylchitobiose as an acceptor substrate than N-acetyl-D-glucosamine.<cite>Ladeveze2013</cite><br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;-mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture of BfMGP<cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bound to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Substitution of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation comletely abolished the activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the scicile glycosidic oxigen<cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the scicile glycosidic oxigen for a direct protonation. Thus the proton relay mechanism described above has been posturated.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensinal structure of BfMGP has been first reported as a characterized enzyme<cite>Nakae2013</cite>. The structures of BfMGP in complex with phosphate; 4-O-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate were determined. The structure of catalytic domain of BfMGP is a five-bladed &beta;-propeller fold. BfMGP forms a homohexamer. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: BfMGP<cite>Senoura2011</cite><br /> ;First general acid residue identification: BfMGP<cite>Nakae2013</cite><br /> ;First sequence identification: BfMGP<cite>Senoura2011</cite><br /> <br /> : Ruminococcus albus &beta;-1,4-mannooligosaccharide phosphorylase<cite>Kawahara2012</cite><br /> <br /> : Bacteroides thetaiotaomicron 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase<cite>Nihira2013</cite> <br /> <br /> : Thermoanaerobacter sp. X-514 1,2-&beta;-oligomannan phosphorylase<cite>Chiku2014</cite> <br /> <br /> : Thermoanaerobacter sp. X-514 &beta;-1,2-mannnobiose phosphorylase <cite>Chiku2014</cite> <br /> <br /> ;First 3-D structure: BfMGP<cite>Nakae2013</cite><br /> <br /> == References ==<br /> <biblio><br /> #Ladeveze2013 pmid=24043624<br /> <br /> #Senoura2011 pmid=21539815<br /> <br /> #Nakae2013 pmid=23954514<br /> <br /> #Kawahara2012 pmid=23093406<br /> <br /> #Nihira2013 pmid=23943617<br /> #Chiku2014 pmid=25500577<br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10512 Glycoside Hydrolase Family 130 2015-02-12T00:53:15Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;-mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase (EC [{{EClink}}2.4.1.319 2.4.1.319]), 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]), 1,2-&beta;-oligomannan phosphorylase, and &beta;-1,2-mannnobiose phosphorylase are members of this family. A GH130 mannoside phosphorylase, unknown human gut bacterium mannoside phosphorylase (UhgbMP), discovered by functional metagenomics of the human gut microbiota, phosphorolyzes 4-O-&beta;-D-mannosyl-N,N'-diacetylchitobiose, and exhibits higher synthetic activity to N,N'-diacetylchitobiose as an acceptor substrate than N-acetyl-D-glucosamine.<cite>Ladeveze2013</cite><br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture of BfMGP<cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bound to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Substitution of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation comletely abolished the activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the scicile glycosidic oxigen<cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the scicile glycosidic oxigen for a direct protonation. Thus the proton relay mechanism described above has been posturated.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensinal structure of BfMGP has been first reported as a characterized enzyme<cite>Nakae2013</cite>. The structures of BfMGP in complex with phosphate; 4-O-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate were determined. The structure of catalytic domain of BfMGP is a five-bladed &beta;-propeller fold. BfMGP forms a homohexamer. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: BfMGP<cite>Senoura2011</cite><br /> ;First general acid residue identification: BfMGP<cite>Nakae2013</cite><br /> ;First sequence identification: BfMGP<cite>Senoura2011</cite><br /> <br /> : Ruminococcus albus &beta;-1,4-mannooligosaccharide phosphorylase<cite>Kawahara2012</cite><br /> <br /> : Bacteroides thetaiotaomicron 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase<cite>Nihira2013</cite> <br /> <br /> : Thermoanaerobacter sp. X-514 1,2-&beta;-oligomannan phosphorylase<cite>Chiku2014</cite> <br /> <br /> : Thermoanaerobacter sp. X-514 &beta;-1,2-mannnobiose phosphorylase <cite>Chiku2014</cite> <br /> <br /> ;First 3-D structure: BfMGP<cite>Nakae2013</cite><br /> <br /> == References ==<br /> <biblio><br /> #Ladeveze2013 pmid=24043624<br /> <br /> #Senoura2011 pmid=21539815<br /> <br /> #Nakae2013 pmid=23954514<br /> <br /> #Kawahara2012 pmid=23093406<br /> <br /> #Nihira2013 pmid=23943617<br /> #Chiku2014 pmid=25500577<br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10511 Glycoside Hydrolase Family 130 2015-02-12T00:52:54Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase (EC [{{EClink}}2.4.1.319 2.4.1.319]), 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]), 1,2-&beta;-oligomannan phosphorylase, and &beta;-1,2-mannnobiose phosphorylase are members of this family. A GH130 mannoside phosphorylase, unknown human gut bacterium mannoside phosphorylase (UhgbMP), discovered by functional metagenomics of the human gut microbiota, phosphorolyzes 4-O-&beta;-D-mannosyl-N,N'-diacetylchitobiose, and exhibits higher synthetic activity to N,N'-diacetylchitobiose as an acceptor substrate than N-acetyl-D-glucosamine.<cite>Ladeveze2013</cite><br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture of BfMGP<cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bound to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Substitution of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation comletely abolished the activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the scicile glycosidic oxigen<cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the scicile glycosidic oxigen for a direct protonation. Thus the proton relay mechanism described above has been posturated.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensinal structure of BfMGP has been first reported as a characterized enzyme<cite>Nakae2013</cite>. The structures of BfMGP in complex with phosphate; 4-O-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate were determined. The structure of catalytic domain of BfMGP is a five-bladed &beta;-propeller fold. BfMGP forms a homohexamer. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: BfMGP<cite>Senoura2011</cite><br /> ;First general acid residue identification: BfMGP<cite>Nakae2013</cite><br /> ;First sequence identification: BfMGP<cite>Senoura2011</cite><br /> <br /> : Ruminococcus albus &beta;-1,4-mannooligosaccharide phosphorylase<cite>Kawahara2012</cite><br /> <br /> : Bacteroides thetaiotaomicron 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase<cite>Nihira2013</cite> <br /> <br /> : Thermoanaerobacter sp. X-514 1,2-&beta;-oligomannan phosphorylase<cite>Chiku2014</cite> <br /> <br /> : Thermoanaerobacter sp. X-514 &beta;-1,2-mannnobiose phosphorylase <cite>Chiku2014</cite> <br /> <br /> ;First 3-D structure: BfMGP<cite>Nakae2013</cite><br /> <br /> == References ==<br /> <biblio><br /> #Ladeveze2013 pmid=24043624<br /> <br /> #Senoura2011 pmid=21539815<br /> <br /> #Nakae2013 pmid=23954514<br /> <br /> #Kawahara2012 pmid=23093406<br /> <br /> #Nihira2013 pmid=23943617<br /> #Chiku2014 pmid=25500577<br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10434 Glycoside Hydrolase Family 130 2015-01-06T00:48:54Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase (EC [{{EClink}}2.4.1.319 2.4.1.319]), 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]), 1,2-&beta;-oligomannan phosphorylase, and &beta;-1,2-mannnobiose phosphorylase are members of this family. A GH130 mannoside phosphorylase, unknown human gut bacterium mannoside phosphorylase (UhgbMP), discovered by functional metagenomics of the human gut microbiota, phosphorolyzes 4-O-&beta;-D-mannosyl-N,N'-diacetylchitobiose, and exhibits higher synthetic activity to N,N'-diacetylchitobiose as an acceptor substrate than N-acetyl-D-glucosamine.<cite>Ladeveze2013</cite><br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture of BfMGP<cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bound to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Substitution of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation comletely abolished the activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the scicile glycosidic oxigen<cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the scicile glycosidic oxigen for a direct protonation. Thus the proton relay mechanism described above has been posturated.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensinal structure of BfMGP has been first reported as a characterized enzyme<cite>Nakae2013</cite>. The structures of BfMGP in complex with phosphate; 4-O-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate were determined. The structure of catalytic domain of BfMGP is a five-bladed &beta;-propeller fold. BfMGP forms a homohexamer. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: BfMGP<cite>Senoura2011</cite><br /> ;First general acid residue identification: BfMGP<cite>Nakae2013</cite><br /> ;First sequence identification: BfMGP<cite>Senoura2011</cite><br /> <br /> : Ruminococcus albus &beta;-1,4-mannooligosaccharide phosphorylase<cite>Kawahara2012</cite><br /> <br /> : Bacteroides thetaiotaomicron 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase<cite>Nihira2013</cite> <br /> <br /> : Thermoanaerobacter sp. X-514 1,2-&beta;-oligomannan phosphorylase<cite>Chiku2014</cite> <br /> <br /> : Thermoanaerobacter sp. X-514 &beta;-1,2-mannnobiose phosphorylase <cite>Chiku2014</cite> <br /> <br /> ;First 3-D structure: BfMGP<cite>Nakae2013</cite><br /> <br /> == References ==<br /> <biblio><br /> #Ladeveze2013 pmid=24043624<br /> <br /> #Senoura2011 pmid=21539815<br /> <br /> #Nakae2013 pmid=23954514<br /> <br /> #Kawahara2012 pmid=23093406<br /> <br /> #Nihira2013 pmid=23943617<br /> #Chiku2014 pmid=25500577<br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10433 Glycoside Hydrolase Family 130 2015-01-06T00:48:19Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase (EC [{{EClink}}2.4.1.319 2.4.1.319]), 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]), 1,2-&beta;-oligomannan phosphorylase, and &beta;-1,2-mannnobiose phosphorylase are members of this family. A GH130 mannoside phosphorylase, unknown human gut bacterium mannoside phosphorylase (UhgbMP), discovered by functional metagenomics of the human gut microbiota, phosphorolyzes 4-O-&beta;-D-mannosyl-N,N'-diacetylchitobiose, and exhibits higher synthetic activity to N,N'-diacetylchitobiose as an acceptor substrate than N-acetyl-D-glucosamine.<cite>Ladeveze2013</cite><br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture of BfMGP<cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bound to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Substitution of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation comletely abolished the activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the scicile glycosidic oxigen<cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the scicile glycosidic oxigen for a direct protonation. Thus the proton relay mechanism described above has been posturated.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensinal structure of BfMGP has been first reported as a characterized enzyme<cite>Nakae2013</cite>. The structures of BfMGP in complex with phosphate; 4-O-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate were determined. The structure of catalytic domain of BfMGP is a five-bladed &beta;-propeller fold. BfMGP forms a homohexamer. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: BfMGP<cite>Senoura2011</cite><br /> ;First general acid residue identification: BfMGP<cite>Nakae2013</cite><br /> ;First sequence identification: BfMGP<cite>Senoura2011</cite><br /> <br /> : Ruminococcus albus &beta;-1,4-mannooligosaccharide phosphorylase<cite>Kawahara2012</cite><br /> <br /> : Bacteroides thetaiotaomicron 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase<cite>Nihira2013</cite> <br /> <br /> : Thermoanaerobacter sp. X-514 1,2-&beta;-oligomannan phosphorylase<cite>Chiku2014</cite> <br /> <br /> : Thermoanaerobacter sp. X-514 &beta;-1,2-mannnobiose phosphorylase <cite>Chiku2014</cite> <br /> <br /> ;First 3-D structure: BfMGP<cite>Nakae2013</cite><br /> .<br /> <br /> == References ==<br /> <biblio><br /> #Ladeveze2013 pmid=24043624<br /> <br /> #Senoura2011 pmid=21539815<br /> <br /> #Nakae2013 pmid=23954514<br /> <br /> #Kawahara2012 pmid=23093406<br /> <br /> #Nihira2013 pmid=23943617<br /> #Chiku2014 pmid=25500577<br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10431 Glycoside Hydrolase Family 130 2015-01-05T04:28:26Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase (EC [{{EClink}}2.4.1.319 2.4.1.319]), 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]), 1,2-&beta;-oligomannan phosphorylase, and &beta;-1,2-mannnobiose phosphorylase are members of this family. A GH130 mannoside phosphorylase, unknown human gut bacterium mannoside phosphorylase (UhgbMP), discovered by functional metagenomics of the human gut microbiota, phosphorolyzes 4-O-&beta;-D-mannosyl-N,N'-diacetylchitobiose, and exhibits higher synthetic activity to N,N'-diacetylchitobiose as an acceptor substrate than N-acetyl-D-glucosamine.<cite>Ladeveze2013</cite><br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture of BfMGP<cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bound to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Substitution of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation comletely abolished the activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the scicile glycosidic oxigen<cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the scicile glycosidic oxigen for a direct protonation. Thus the proton relay mechanism described above has been posturated.<br /> <br /> <br /> == Three-dimensional structures ==<br /> Three-dimensinal structure of BfMGP has been first reported as a characterized enzyme<cite>Nakae2013</cite>. The structures of BfMGP in complex with phosphate; 4-O-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate were determined. The structure of catalytic domain of BfMGP is a five-bladed &beta;-propeller fold. BfMGP forms a homohexamer. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: BfMGP<cite>Senoura2011</cite><br /> ;First general acid residue identification: BfMGP<cite>Nakae2013</cite><br /> ;First sequence identification: BfMGP<cite>Senoura2011</cite><br /> <br /> : Ruminococcus albus &beta;-1,4-mannooligosaccharide phosphorylase<cite>Kawahara2012</cite><br /> <br /> : Bacteroides thetaiotaomicron 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase<cite>Nihira2013</cite> <br /> <br /> : Thermoanaerobacter sp. X-514 1,2-&beta;-oligomannan phosphorylase<cite>Chiku2014</cite> <br /> <br /> : Thermoanaerobacter sp. X-514 &beta;-1,2-mannnobiose phosphorylase <cite>Chiku2014</cite> <br /> <br /> ;First 3-D structure: BfMGP<cite>Nakae2013</cite><br /> .<br /> <br /> == References ==<br /> <biblio><br /> #Ladeveze2013 pmid=24043624<br /> <br /> #Senoura2011 pmid=21539815<br /> <br /> #Nakae2013 pmid=23954514<br /> <br /> #Kawahara2012 pmid=23093406<br /> <br /> #Nihira2013 pmid=23943617<br /> #Chiku2014 pmid=25500577<br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10430 Glycoside Hydrolase Family 130 2015-01-05T04:27:56Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]), 1,2-&beta;-oligomannan phosphorylase, and &beta;-1,2-mannnobiose phosphorylase are members of this family. A GH130 mannoside phosphorylase, unknown human gut bacterium mannoside phosphorylase (UhgbMP), discovered by functional metagenomics of the human gut microbiota, phosphorolyzes 4-O-&beta;-D-mannosyl-N,N'-diacetylchitobiose, and exhibits higher synthetic activity to N,N'-diacetylchitobiose as an acceptor substrate than N-acetyl-D-glucosamine.<cite>Ladeveze2013</cite><br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture of BfMGP<cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bound to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Substitution of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation comletely abolished the activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the scicile glycosidic oxigen<cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the scicile glycosidic oxigen for a direct protonation. Thus the proton relay mechanism described above has been posturated.<br /> <br /> <br /> == Three-dimensional structures ==<br /> Three-dimensinal structure of BfMGP has been first reported as a characterized enzyme<cite>Nakae2013</cite>. The structures of BfMGP in complex with phosphate; 4-O-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate were determined. The structure of catalytic domain of BfMGP is a five-bladed &beta;-propeller fold. BfMGP forms a homohexamer. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: BfMGP<cite>Senoura2011</cite><br /> ;First general acid residue identification: BfMGP<cite>Nakae2013</cite><br /> ;First sequence identification: BfMGP<cite>Senoura2011</cite><br /> <br /> : Ruminococcus albus &beta;-1,4-mannooligosaccharide phosphorylase<cite>Kawahara2012</cite><br /> <br /> : Bacteroides thetaiotaomicron 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase<cite>Nihira2013</cite> <br /> <br /> : Thermoanaerobacter sp. X-514 1,2-&beta;-oligomannan phosphorylase<cite>Chiku2014</cite> <br /> <br /> : Thermoanaerobacter sp. X-514 &beta;-1,2-mannnobiose phosphorylase <cite>Chiku2014</cite> <br /> <br /> ;First 3-D structure: BfMGP<cite>Nakae2013</cite><br /> .<br /> <br /> == References ==<br /> <biblio><br /> #Ladeveze2013 pmid=24043624<br /> <br /> #Senoura2011 pmid=21539815<br /> <br /> #Nakae2013 pmid=23954514<br /> <br /> #Kawahara2012 pmid=23093406<br /> <br /> #Nihira2013 pmid=23943617<br /> #Chiku2014 pmid=25500577<br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10429 Glycoside Hydrolase Family 130 2015-01-05T03:22:26Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]), 1,2-&beta;-oligomannan phosphorylase, and &beta;1,2-mannnobiose phosphorylase are members of this family. A GH130 mannoside phosphorylase, unknown human gut bacterium mannoside phosphorylase (UhgbMP), discovered by functional metagenomics of the human gut microbiota, phosphorolyzes 4-O-&beta;-D-mannosyl-N,N'-diacetylchitobiose, and exhibits higher synthetic activity to N,N'-diacetylchitobiose as an acceptor substrate than N-acetyl-D-glucosamine.<cite>Ladeveze2013</cite><br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture of BfMGP<cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bond to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Substitution of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation comletely abolished the activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the scicile glycosidic oxigen<cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the scicile glycosidic oxigen for a direct protonation. Thus the proton relay mechanism described above has been posturated.<br /> <br /> <br /> == Three-dimensional structures ==<br /> Three-dimensinal structure of BfMGP has been first reported as a characterized enzyme<cite>Nakae2013</cite>. The structures of BfMGP in complex with phosphate; 4-O-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate were determined. The structure of catalytic domain of BfMGP is a five-bladed &beta;-propeller fold. BfMGP forms a homohexamer. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: BfMGP<cite>Senoura2011</cite><br /> ;First general acid residue identification: BfMGP<cite>Nakae2013</cite><br /> ;First sequence identification: BfMGP<cite>Senoura2011</cite><br /> <br /> : Ruminococcus albus &beta;-1,4-mannooligosaccharide phosphorylase<cite>Kawahara2012</cite><br /> <br /> : Bacteroides thetaiotaomicron 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase<cite>Nihira2013</cite> <br /> ;First 3-D structure: BfMGP<cite>Nakae2013</cite><br /> .<br /> <br /> == References ==<br /> <biblio><br /> #Ladeveze2013 pmid=24043624<br /> <br /> #Senoura2011 pmid=21539815<br /> <br /> #Nakae2013 pmid=23954514<br /> <br /> #Kawahara2012 pmid=23093406<br /> <br /> #Nihira2013 pmid=23943617<br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=User:Wataru_Saburi&diff=10390 User:Wataru Saburi 2014-12-05T03:07:11Z

<p>Wataru Saburi: </p> <hr /> <div>[[<br /> <br /> Image:Saburi2.jpg|200px|right]]<br /> <br /> '''Wataru Saburi''' is an assistant professor at Laboratory of Biochemistry in Research Faculty of Agriculture, Hokkaido University (Sapporo, Japan). He obtained Ph. D from Graduate School of Agriculture, Hokkaido University in 2006, under the supervision of Professor Atsuo Kimura. He joined the Research Institute of Nihon Shokuhin Kako Co. Ltd. as a researcher (2006-2010), and developed functional oligosaccharides produced from starch. His research interests are structures and functions of carbohydrate active enzymes and efficient synthesis of functional oligosaccharides. He has studied about<br /> <br /> * [[GH1]] rice β-glucosidase <cite>Himeno2013</cite><br /> * [[GH13]] Bacillus sp. AAH-31 α-amylase <cite>Kim2012 Saburia2013</cite><br /> * [[GH13]] Streptococcus mutans dextran glucosidase <cite>Saburi2006 Saburi2007 Hondoh2008 Kobayashi2011 Saburib2013</cite><br /> * [[GH13]] Halomonas sp. H11 α-glucosidase <cite>Ojima2012</cite><br /> * [[GH13]] Bacillus clarkii γ-cyclodextrinase <cite>Nakagawa2008</cite><br /> <br /> * [[GH31]] Bacillus sp. AHU 2001 α-glucosidase BspAG31A <cite>Saburi2014</cite><br /> * [[GH94]] Ruminococcus albus cellobiose phosphorylase <cite>Hamura2012 Hamura2013</cite><br /> * [[GH94]] Ruminococcus albus cellodextrin phosphorylase <cite>Sawano2013</cite><br /> * [[GH130]] Ruminococcus albus 4-O-β-mannosylglucose phosphorylase (RaMP1) <cite>Kawahara2012</cite><br /> * [[GH130]] Rhodothermus marinus 4-O-β-mannosylglucose phosphorylase <cite>Jaito2014</cite><br /> * [[GH130]] Ruminococcus albus β-1,4-mannooligosaccharide phosphorylase (RaMP2) <cite>Kawahara2012</cite><br /> <br /> <br /> <br /> ----<br /> <br /> <biblio><br /> #Himeno2013 pmid=23649259<br /> #>Kim2012 pmid=22785486<br /> #>Saburia2013 pmid=24018662<br /> #>Saburi2006 pmid=16503208<br /> #>Saburi2007 pmid=17768352<br /> <br /> #>Hondoh2008 pmid=18395742<br /> <br /> #>Kobayashi2011 pmid=21821929<br /> #>Saburib2013 pmid=24052257<br /> #>Ojima2012 pmid=22226947<br /> #>Nakagawa2008 pmid=18824139<br /> #>Saburi2014 pmid=25450253<br /> #>Hamura2012 pmid=22484959<br /> <br /> #>Hamura2013 pmid=23845516<br /> #>Sawano2013 pmid=23802549<br /> #>Kawahara2012 pmid=23093406<br /> #>Jaito2014 pmid=25036679<br /> <br /> <br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Contributors|Saburi,Wataru]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10389 Glycoside Hydrolase Family 130 2014-12-05T00:20:23Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family. A GH130 mannoside phosphorylase, unknown human gut bacterium mannoside phosphorylase (UhgbMP), discovered by functional metagenomics of the human gut microbiota, phosphorolyzes 4-O-&beta;-D-mannosyl-N,N'-diacetylchitobiose, and exhibits higher synthetic activity to N,N'-diacetylchitobiose as an acceptor substrate than N-acetyl-D-glucosamine.<cite>Ladeveze2013</cite><br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture of BfMGP<cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bond to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Substitution of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation comletely abolished the activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the scicile glycosidic oxigen<cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the scicile glycosidic oxigen for a direct protonation. Thus the proton relay mechanism described above has been posturated.<br /> <br /> <br /> == Three-dimensional structures ==<br /> Three-dimensinal structure of BfMGP has been first reported as a characterized enzyme<cite>Nakae2013</cite>. The structures of BfMGP in complex with phosphate; 4-O-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate were determined. The structure of catalytic domain of BfMGP is a five-bladed &beta;-propeller fold. BfMGP forms a homohexamer. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: BfMGP<cite>Senoura2011</cite><br /> ;First general acid residue identification: BfMGP<cite>Nakae2013</cite><br /> ;First sequence identification: BfMGP<cite>Senoura2011</cite><br /> <br /> : Ruminococcus albus &beta;-1,4-mannooligosaccharide phosphorylase<cite>Kawahara2012</cite><br /> <br /> : Bacteroides thetaiotaomicron 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase<cite>Nihira2013</cite> <br /> ;First 3-D structure: BfMGP<cite>Nakae2013</cite><br /> .<br /> <br /> == References ==<br /> <biblio><br /> #Ladeveze2013 pmid=24043624<br /> <br /> #Senoura2011 pmid=21539815<br /> <br /> #Nakae2013 pmid=23954514<br /> <br /> #Kawahara2012 pmid=23093406<br /> <br /> #Nihira2013 pmid=23943617<br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10388 Glycoside Hydrolase Family 130 2014-12-05T00:17:23Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family. A GH130 mannoside phosphorylase, unknown human gut bacterium mannoside phosphorylase (UhgbMP), discovered by functional metagenomics of the human gut microbiota, phosphorolyzes 4-O-&beta;-D-mannosyl-N,N'-diacetylchitobiose, and exhibits higher synthetic activity to N,N'-diacetylchitobiose as an acceptor substrate than N-acetyl-D-glucosamine.<cite>Ladeveze2013</cite><br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture of BfMGP<cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bond to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Substitution of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation comletely abolished the activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the scicile glycosidic oxigen<cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the scicile glycosidic oxigen for a direct protonation. Thus the proton relay mechanism described above has been posturated.<br /> <br /> <br /> == Three-dimensional structures ==<br /> Three-dimensinal structure of BfMGP has been first reported as a characterized enzyme<cite>Nakae2013</cite>. The structures of BfMGP in complex with phosphate; 4-O-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate were determined. The structure of catalytic domain of BfMGP is a five-bladed &beta;-propeller fold. BfMGP forms a homohexamer. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: BfMGP<cite>Senoura2011</cite><br /> ;First general acid residue identification: BfMGP<cite>Nakae2013</cite><br /> ;First sequence identification: 4-O-&beta;-D-mannosyl-D-glucose phosphorylase<cite>Senoura2011</cite><br /> <br /> : Ruminococcus albus &beta;-1,4-mannooligosaccharide phosphorylase<cite>Kawahara2012</cite><br /> <br /> : Bacteroides thetaiotaomicron 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase<cite>Nihira2013</cite> <br /> ;First 3-D structure: BfMGP<cite>Nakae2013</cite><br /> .<br /> <br /> == References ==<br /> <biblio><br /> #Ladeveze2013 pmid=24043624<br /> <br /> #Senoura2011 pmid=24539815<br /> <br /> #Nakae2013 pmid=23954514<br /> <br /> #Kawahara2012 pmid=23093406<br /> <br /> #Nihira2013 pmid=23943617<br /> <br /> #Cantarel2009 pmid=18838391<br /> #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10387 Glycoside Hydrolase Family 130 2014-12-05T00:12:35Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family. A GH130 mannoside phosphorylase, unknown human gut bacterium mannoside phosphorylase (UhgbMP), discovered by functional metagenomics of the human gut microbiota, phosphorolyzes 4-O-&beta;-D-mannosyl-N,N'-diacetylchitobiose, and exhibits higher synthetic activity to N,N'-diacetylchitobiose as an acceptor substrate than N-acetyl-D-glucosamine.<cite>Ladeveze2013</cite><br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture of BfMGP<cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bond to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Substitution of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation comletely abolished the activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the scicile glycosidic oxigen<cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the scicile glycosidic oxigen for a direct protonation. Thus the proton relay mechanism described above has been posturated.<br /> <br /> <br /> == Three-dimensional structures ==<br /> Three-dimensinal structure of BfMGP has been first reported as a characterized enzyme<cite>Nakae2013</cite>. The structures of BfMGP in complex with phosphate; 4-O-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate were determined. The structure of catalytic domain of BfMGP is a five-bladed &beta;-propeller fold. BfMGP forms a homohexamer. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: BfMGP<cite>Senoura2011</cite><br /> ;First general acid residue identification: BfMGP<cite>Nakae2013</cite><br /> ;First sequence identification: 4-O-&beta;-D-mannosyl-D-glucose phosphorylase<cite>Senoura2011</cite><br /> <br /> : Ruminococcus albus &beta;-1,4-mannooligosaccharide phosphorylase<cite>Kawahara2012</cite><br /> <br /> : Bacteroides thetaiotaomicron 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase<cite>Nihira2013</cite> <br /> ;First 3-D structure: BfMGP<cite>Nakae2013</cite><br /> .<br /> <br /> == References ==<br /> <biblio><br /> #Cantarel2009 pmid=18838391<br /> #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10386 Glycoside Hydrolase Family 130 2014-12-05T00:11:38Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family. A GH130 mannoside phosphorylase, unknown human gut bacterium mannoside phosphorylase (UhgbMP), discovered by functional metagenomics of the human gut microbiota, phosphorolyzes 4-O-&beta;-D-mannosyl-N,N'-diacetylchitobiose, and exhibits higher synthetic activity to N,N'-diacetylchitobiose as an acceptor substrate than N-acetyl-D-glucosamine.<cite>Ladeveze2013</cite><br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture of BfMGP<cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bond to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Substitution of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation comletely abolished the activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the scicile glycosidic oxigen<cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the scicile glycosidic oxigen for a direct protonation. Thus the proton relay mechanism described above has been posturated.<br /> <br /> <br /> == Three-dimensional structures ==<br /> Three-dimensinal structure of BfMGP has been first reported as a characterized enzyme<cite>Nakae2013</cite>. The structures of BfMGP in complex with phosphate; 4-O-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate were determined. The structure of catalytic domain of BfMGP is a five-bladed &beta;-propeller fold. BfMGP forms a homohexamer. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: BfMGP<cite>Senoura2011</cite><br /> ;First general acid residue identification: BfMGP<cite>Nakae2013</cite><br /> ;First sequence identification: 4-O-&beta;-D-mannosyl-D-glucose phosphorylase<cite>Senoura2011</cite>:Ruminococcus albus &beta;-1,4-mannooligosaccharide phosphorylase<cite>Kawahara2012</cite>:Bacteroides thetaiotaomicron 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase<cite>Nihira2013</cite> <br /> ;First 3-D structure: BfMGP<cite>Nakae2013</cite><br /> .<br /> <br /> == References ==<br /> <biblio><br /> #Cantarel2009 pmid=18838391<br /> #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10385 Glycoside Hydrolase Family 130 2014-12-05T00:09:56Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family. A GH130 mannoside phosphorylase, unknown human gut bacterium mannoside phosphorylase (UhgbMP), discovered by functional metagenomics of the human gut microbiota, phosphorolyzes 4-O-&beta;-D-mannosyl-N,N'-diacetylchitobiose, and exhibits higher synthetic activity to N,N'-diacetylchitobiose as an acceptor substrate than N-acetyl-D-glucosamine.<cite>Ladeveze2013</cite><br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture of BfMGP<cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bond to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Substitution of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation comletely abolished the activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the scicile glycosidic oxigen<cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the scicile glycosidic oxigen for a direct protonation. Thus the proton relay mechanism described above has been posturated.<br /> <br /> <br /> == Three-dimensional structures ==<br /> Three-dimensinal structure of BfMGP has been first reported as a characterized enzyme<cite>Nakae2013</cite>. The structures of BfMGP in complex with phosphate; 4-O-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate were determined. The structure of catalytic domain of BfMGP is a five-bladed &beta;-propeller fold. BfMGP forms a homohexamer. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: BfMGP<cite>Senoura2011</cite>.<br /> ;First general acid residue identification: BfMGP<cite>Nakae2013</cite>.<br /> ;First sequence identification: 4-O-&beta;-D-mannosyl-D-glucose phosphorylase<cite>Senoura2011</cite>.<br /> <br /> Ruminococcus albus &beta;-1,4-mannooligosaccharide phosphorylase<cite>Kawahara2012</cite>.<br /> <br /> Bacteroides thetaiotaomicron 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase<cite>Nihira2013</cite>. <br /> ;First 3-D structure: BfMGP<cite>Nakae2013</cite>.<br /> .<br /> <br /> == References ==<br /> <biblio><br /> #Cantarel2009 pmid=18838391<br /> #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10384 Glycoside Hydrolase Family 130 2014-12-05T00:04:18Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family. A GH130 mannoside phosphorylase, unknown human gut bacterium mannoside phosphorylase (UhgbMP), discovered by functional metagenomics of the human gut microbiota, phosphorolyzes 4-O-&beta;-D-mannosyl-N,N'-diacetylchitobiose, and exhibits higher synthetic activity to N,N'-diacetylchitobiose as an acceptor substrate than N-acetyl-D-glucosamine.<cite>Ladeveze2013</cite><br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' (BfMGP) produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture of BfMGP<cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in BfMGP) donates a proton to O3 of mannosyl group bond to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Substitution of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation comletely abolished the activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of BfMGP, corresponding to Asp104 of UhgbMP, is situated near the scicile glycosidic oxigen<cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the scicile glycosidic oxigen for a direct protonation. Thus the proton relay mechanism described above has been posturated.<br /> <br /> <br /> == Three-dimensional structures ==<br /> Three-dimensinal structure of BfMGP has been first reported as a characterized enzyme<cite>Nakae2013</cite>. The structures of BfMGP in complex with phosphate; 4-O-&beta;-D-mannosyl-D-glucose and phosphate; mannose, glucose, and phosphate; and &alpha;-mannose 1-phosphate were determined. The structure of catalytic domain of BfMGP is a five-bladed &beta;-propeller fold. BfMGP forms a homohexamer. It has long &alpha;-helices at the N- and C-termini, and these structure are predicted to be responsible for the quaternary structure formation.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: BfMGP<cite>Senoura2011</cite>.<br /> ;First general acid residue identification: BfMGP<cite>Nakae2013</cite>.<br /> ;First sequence identification: 4-O-&beta;-D-mannosyl-D-glucose phosphorylase .<br /> ;First 3-D structure: Content is to be added here.<br /> <br /> == References ==<br /> <biblio><br /> #Cantarel2009 pmid=18838391<br /> #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10383 Glycoside Hydrolase Family 130 2014-12-04T23:23:58Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family. A mannoside phosphorylase, unknown human gut bacterium mannoside phosphorylase (UhgbMP), discovered by functional metagenomics of the human gut microbiota, phosphorolyzes 4-O-&beta;-D-Mannosyl-N,N'-diacetylchitobiose, and exhibits higher synthetic activity to N,N'-diacetylchitobiose as an acceptor substrate than N-acetyl-D-glucosamine.<cite>Ladeveze2013</cite><br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture of ''B. fragilis'' 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase <cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in ''B. fragilis'' 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase) donates a proton to O3 of mannosyl group bond to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Substitution of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation comletely abolished the activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of B. fragilis 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase, corresponding to Asp104 of UhgbMP, is situated near the scicile glycosidic oxigen<cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the scicile glycosidic oxigen for a direct protonation. Thus the proton relay mechanism described above has been posturated.<br /> <br /> <br /> == Three-dimensional structures ==<br /> Content is to be added here.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Content is to be added here.<br /> ;First catalytic nucleophile identification: Content is to be added here.<br /> ;First general acid/base residue identification: Content is to be added here.<br /> ;First 3-D structure: Content is to be added here.<br /> <br /> == References ==<br /> <biblio><br /> #Cantarel2009 pmid=18838391<br /> #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10382 Glycoside Hydrolase Family 130 2014-12-04T23:22:43Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family. A mannoside phosphorylase, unknown human gut bacterium mannoside phosphorylase (UhgbMP), discovered by functional metagenomics of the human gut microbiota, phosphorolyzes 4-O-&beta;-D-Mannosyl-N,N'-diacetylchitobiose, and exhibits higher synthetic activity to N,N'-diacetylchitobiose as an acceptor substrate than N-acetyl-D-glucosamine.<cite>Ladeveze2013</cite><br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-Mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture of ''B. fragilis'' 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase <cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in ''B. fragilis'' 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase) donates a proton to O3 of mannosyl group bond to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> <br /> == Catalytic Residues ==<br /> Ladevèze et al. <cite>Ladeveze2013</cite> compared 369 protein sequences of GH130 members and selected Asp104, Glu273, and Asp304 of UhgbMP as putative catalytic amino acid residues. Substitution of these acidic amino acid residues resulted in large reduction of enzyme activity. Especially, the D104N mutation comletely abolished the activity. Consistent with this result, three dimensional structure analysis demonstrated that only Asp131 of B. fragilis 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase, corresponding to Asp104 of UhgbMP, is situated near the scicile glycosidic oxigen<cite>Nakae2013</cite>. However, this Asp appeared to be too distant from the the scicile glycosidic oxigen for a direct protonation. Thus the proton relay mechanism described above has been posturated.<br /> <br /> <br /> == Three-dimensional structures ==<br /> Content is to be added here.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Content is to be added here.<br /> ;First catalytic nucleophile identification: Content is to be added here.<br /> ;First general acid/base residue identification: Content is to be added here.<br /> ;First 3-D structure: Content is to be added here.<br /> <br /> == References ==<br /> <biblio><br /> #Cantarel2009 pmid=18838391<br /> #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10381 Glycoside Hydrolase Family 130 2014-11-19T02:31:43Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |inverting<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family.<br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-Mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture analysis of ''B. fragilis'' 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase <cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in ''B. fragilis'' 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase) donates a proton to O3 of mannosyl group bond to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> == Catalytic Residues ==<br /> Content is to be added here.<br /> <br /> == Three-dimensional structures ==<br /> Content is to be added here.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Content is to be added here.<br /> ;First catalytic nucleophile identification: Content is to be added here.<br /> ;First general acid/base residue identification: Content is to be added here.<br /> ;First 3-D structure: Content is to be added here.<br /> <br /> == References ==<br /> <biblio><br /> #Cantarel2009 pmid=18838391<br /> #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10380 Glycoside Hydrolase Family 130 2014-11-17T02:34:52Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |retaining/inverting<br /> |-<br /> |'''Active site residues'''<br /> |known/not known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family.<br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-Mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture analysis of ''B. fragilis'' 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase <cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in ''B. fragilis'' 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase) donates a proton to O3 of mannosyl group bond to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> == Catalytic Residues ==<br /> Content is to be added here.<br /> <br /> == Three-dimensional structures ==<br /> Content is to be added here.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Content is to be added here.<br /> ;First catalytic nucleophile identification: Content is to be added here.<br /> ;First general acid/base residue identification: Content is to be added here.<br /> ;First 3-D structure: Content is to be added here.<br /> <br /> == References ==<br /> <biblio><br /> #Cantarel2009 pmid=18838391<br /> #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10379 Glycoside Hydrolase Family 130 2014-11-17T02:30:06Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |retaining/inverting<br /> |-<br /> |'''Active site residues'''<br /> |known/not known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family.<br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-Mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture analysis of ''B. fragilis'' 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase <cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, in which the general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in ''B. fragilis'' 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase) donates a proton to O3 of mannosyl group bond to subsite -1, and a proton is donated to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and &alpha;-mannose 1-phosphate is generated.<br /> == Catalytic Residues ==<br /> Content is to be added here.<br /> <br /> == Three-dimensional structures ==<br /> Content is to be added here.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Content is to be added here.<br /> ;First catalytic nucleophile identification: Content is to be added here.<br /> ;First general acid/base residue identification: Content is to be added here.<br /> ;First 3-D structure: Content is to be added here.<br /> <br /> == References ==<br /> <biblio><br /> #Cantarel2009 pmid=18838391<br /> #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10378 Glycoside Hydrolase Family 130 2014-11-17T02:14:03Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |retaining/inverting<br /> |-<br /> |'''Active site residues'''<br /> |known/not known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family.<br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase produces &alpha;-mannose 1-phosphate and glucose from 4-O-&beta;-D-Mannosyl-D-glucose and inorganic phosphate.<br /> <br /> == Catalytic Residues ==<br /> Content is to be added here.<br /> <br /> == Three-dimensional structures ==<br /> Content is to be added here.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Content is to be added here.<br /> ;First catalytic nucleophile identification: Content is to be added here.<br /> ;First general acid/base residue identification: Content is to be added here.<br /> ;First 3-D structure: Content is to be added here.<br /> <br /> == References ==<br /> <biblio><br /> #Cantarel2009 pmid=18838391<br /> #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10377 Glycoside Hydrolase Family 130 2014-11-17T00:29:06Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |retaining/inverting<br /> |-<br /> |'''Active site residues'''<br /> |known/not known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family.<br /> == Kinetics and Mechanism ==<br /> GH130 phosphorylases phosphorolyze &beta;1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <br /> <br /> == Catalytic Residues ==<br /> Content is to be added here.<br /> <br /> == Three-dimensional structures ==<br /> Content is to be added here.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Content is to be added here.<br /> ;First catalytic nucleophile identification: Content is to be added here.<br /> ;First general acid/base residue identification: Content is to be added here.<br /> ;First 3-D structure: Content is to be added here.<br /> <br /> == References ==<br /> <biblio><br /> #Cantarel2009 pmid=18838391<br /> #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10368 Glycoside Hydrolase Family 130 2014-10-23T22:47:52Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |retaining/inverting<br /> |-<br /> |'''Active site residues'''<br /> |known/not known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family.<br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> == Catalytic Residues ==<br /> Content is to be added here.<br /> <br /> == Three-dimensional structures ==<br /> Content is to be added here.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Content is to be added here.<br /> ;First catalytic nucleophile identification: Content is to be added here.<br /> ;First general acid/base residue identification: Content is to be added here.<br /> ;First 3-D structure: Content is to be added here.<br /> <br /> == References ==<br /> <biblio><br /> #Cantarel2009 pmid=18838391<br /> #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10367 Glycoside Hydrolase Family 130 2014-10-23T22:47:08Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |retaining/inverting<br /> |-<br /> |'''Active site residues'''<br /> |known/not known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family.<br /> <br /> Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''<br /> <br /> In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.<br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> == Catalytic Residues ==<br /> Content is to be added here.<br /> <br /> == Three-dimensional structures ==<br /> Content is to be added here.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Content is to be added here.<br /> ;First catalytic nucleophile identification: Content is to be added here.<br /> ;First general acid/base residue identification: Content is to be added here.<br /> ;First 3-D structure: Content is to be added here.<br /> <br /> == References ==<br /> <biblio><br /> #Cantarel2009 pmid=18838391<br /> #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10366 Glycoside Hydrolase Family 130 2014-10-23T22:46:24Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |retaining/inverting<br /> |-<br /> |'''Active site residues'''<br /> |known/not known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> [[GH130]] contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family.<br /> <br /> Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''<br /> <br /> In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.<br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> == Catalytic Residues ==<br /> Content is to be added here.<br /> <br /> == Three-dimensional structures ==<br /> Content is to be added here.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Content is to be added here.<br /> ;First catalytic nucleophile identification: Content is to be added here.<br /> ;First general acid/base residue identification: Content is to be added here.<br /> ;First 3-D structure: Content is to be added here.<br /> <br /> == References ==<br /> <biblio><br /> #Cantarel2009 pmid=18838391<br /> #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_130&diff=10365 Glycoside Hydrolase Family 130 2014-10-23T22:45:48Z

<p>Wataru Saburi: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Wataru Saburi^^^<br /> * [[Responsible Curator]]: ^^^Haruhide Mori^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH130'''<br /> |-<br /> |'''Clan''' <br /> |GH-x<br /> |-<br /> |'''Mechanism'''<br /> |retaining/inverting<br /> |-<br /> |'''Active site residues'''<br /> |known/not known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |{{CAZyDBlink}}GH130.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> GH130 contains phosphorylases catalyzing the phosphorolysis of &beta;1-4mannosidic linkage at the non-reducing end of substrates. 4-O-&beta;-D-mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), &beta;-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-&beta;-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family.<br /> <br /> Authors may get an idea of what to put in each field from ''Curator Approved'' [[Glycoside Hydrolase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''<br /> <br /> In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.<br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> == Catalytic Residues ==<br /> Content is to be added here.<br /> <br /> == Three-dimensional structures ==<br /> Content is to be added here.<br /> <br /> == Family Firsts ==<br /> ;First stereochemistry determination: Content is to be added here.<br /> ;First catalytic nucleophile identification: Content is to be added here.<br /> ;First general acid/base residue identification: Content is to be added here.<br /> ;First 3-D structure: Content is to be added here.<br /> <br /> == References ==<br /> <biblio><br /> #Cantarel2009 pmid=18838391<br /> #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]<br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH130]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=User_talk:Wataru_Saburi&diff=10327 User talk:Wataru Saburi 2014-10-13T22:23:19Z

<p>Wataru Saburi: Blanked the page</p> <hr /> <div></div>

Wataru Saburi https://www.cazypedia.org/index.php?title=User:Wataru_Saburi&diff=10326 User:Wataru Saburi 2014-10-13T22:23:01Z

<p>Wataru Saburi: </p> <hr /> <div><br /> <br /> [[Image:Saburi2.jpg]]<br /> <br /> '''Wataru Saburi''' is an assistant professor at Laboratory of Biochemistry in Research Faculty of Agriculture, Hokkaido University (Sapporo, Japan). He obtained Ph. D from Graduate School of Agriculture, Hokkaido University in 2006, under the supervision of Professor Atsuo Kimura. He joined the Research Institute of Nihon Shokuhin Kako Co. Ltd. as a researcher (2006-2010), and developed functional oligosaccharides produced from starch. His research interests are structures and functions of carbohydrate active enzymes and efficient synthesis of functional oligosaccharides. He has studied about<br /> <br /> * [[GH1]] rice β-glucosidase <cite>Himeno2013</cite><br /> * [[GH13]] Bacillus sp. AAH-31 α-amylase <cite>Kim2012 Saburia2013</cite><br /> * [[GH13]] Streptococcus mutans dextran glucosidase <cite>Saburi2006 Saburi2007 Hondoh2008 Kobayashi2011 Saburib2013</cite><br /> * [[GH13]] Halomonas sp. H11 α-glucosidase <cite>Ojima2012</cite><br /> * [[GH13]] Bacillus clarkii γ-cyclodextrinase <cite>Nakagawa2008</cite><br /> * [[GH94]] Ruminococcus albus cellobiose phosphorylase <cite>Hamura2012 Hamura2013</cite><br /> * [[GH94]] Ruminococcus albus cellodextrin phosphorylase <cite>Sawano2013</cite><br /> * [[GH130]] Ruminococcus albus 4-O-β-mannosylglucose phosphorylase (RaMP1) <cite>Kawahara2012</cite><br /> * [[GH130]] Rhodothermus marinus 4-O-β-mannosylglucose phosphorylase <cite>Jaito2014</cite><br /> * [[GH130]] Ruminococcus albus β-1,4-mannooligosaccharide phosphorylase (RaMP2) <cite>Kawahara2012</cite><br /> <br /> <br /> <br /> ----<br /> <br /> <biblio><br /> #Himeno2013 pmid=23649259<br /> #>Kim2012 pmid=22785486<br /> #>Saburia2013 pmid=24018662<br /> #>Saburi2006 pmid=16503208<br /> #>Saburi2007 pmid=17768352<br /> <br /> #>Hondoh2008 pmid=18395742<br /> <br /> #>Kobayashi2011 pmid=21821929<br /> #>Saburib2013 pmid=24052257<br /> #>Ojima2012 pmid=22226947<br /> #>Nakagawa2008 pmid=18824139<br /> <br /> #>Hamura2012 pmid=22484959<br /> <br /> #>Hamura2013 pmid=23845516<br /> #>Sawano2013 pmid=23802549<br /> #>Kawahara2012 pmid=23093406<br /> #>Jaito2014 pmid=25036679<br /> <br /> <br /> <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Contributors|Saburi,Wataru]]</div>

Wataru Saburi https://www.cazypedia.org/index.php?title=User_talk:Wataru_Saburi&diff=10325 User talk:Wataru Saburi 2014-10-13T13:47:48Z

<p>Wataru Saburi: </p> <hr /> <div><br /> <br /> [[Image:Saburi2.jpg]]<br /> <br /> '''Wataru Saburi''' is an assistant professor at Laboratory of Biochemistry in Research Faculty of Agriculture, Hokkaido University (Sapporo, Japan). He obtained Ph. D from Graduate School of Agriculture, Hokkaido University in 2006, under the supervision of Professor Atsuo Kimura. He joined the Research Institute of Nihon Shokuhin Kako Co. Ltd. as a researcher (2006-2010), and developed functional oligosaccharides produced from starch. His research interests are structures and functions of carbohydrate active enzymes and efficient synthesis of functional oligosaccharides. He has studied about<br /> <br /> * [[GH1]] rice β-glucosidase <cite>Himeno2013</cite><br /> * [[GH13]] Bacillus sp. AAH-31 α-amylase <cite>Kim2012 Saburia2013</cite><br /> * [[GH13]] Streptococcus mutans dextran glucosidase <cite>Saburi2006 Saburi2007 Hondoh2008 Kobayashi2011 Saburib2013</cite><br /> * [[GH13]] Halomonas sp. H11 α-glucosidase <cite>Ojima2012</cite><br /> * [[GH13]] Bacillus clarkii γ-cyclodextrinase <cite>Nakagawa2008</cite><br /> * [[GH94]] Ruminococcus albus cellobiose phosphorylase <cite>Hamura2012 Hamura2013</cite><br /> * [[GH94]] Ruminococcus albus cellodextrin phosphorylase <cite>Sawano2013</cite><br /> * [[GH130]] Ruminococcus albus 4-O-β-mannosylglucose phosphorylase (RaMP1) <cite>Kawahara2012</cite><br /> * [[GH130]] Rhodothermus marinus 4-O-β-mannosylglucose phosphorylase <cite>Jaito2014</cite><br /> * [[GH130]] Ruminococcus albus β-1,4-mannooligosaccharide phosphorylase (RaMP2) <cite>Kawahara2012</cite><br /> <br /> <br /> <br /> ----<br /> <br /> <biblio><br /> #Himeno2013 pmid=23649259<br /> #>Kim2012 pmid=22785486<br /> #>Saburia2013 pmid=24018662<br /> #>Saburi2006 pmid=16503208<br /> #>Saburi2007 pmid=17768352<br /> <br /> #>Hondoh2008 pmid=18395742<br /> <br /> #>Kobayashi2011 pmid=21821929<br /> #>Saburib2013 pmid=24052257<br /> #>Ojima2012 pmid=22226947<br /> #>Nakagawa2008 pmid=18824139<br /> <br /> #>Hamura2012 pmid=22484959<br /> <br /> #>Hamura2013 pmid=23845516<br /> #>Sawano2013 pmid=23802549<br /> #>Kawahara2012 pmid=23093406<br /> #>Jaito2014 pmid=25036679<br /> <br /> <br /> <br /> </biblio><br /> <br /> <br /> [[Category:Contributors|Lastname,Firstname]]<br /> </div>

Wataru Saburi https://www.cazypedia.org/index.php?title=User_talk:Wataru_Saburi&diff=10324 User talk:Wataru Saburi 2014-10-13T13:43:23Z

<p>Wataru Saburi: </p> <hr /> <div><br /> <br /> [[Image:Saburi2.jpg]]<br /> <br /> '''Wataru Saburi''' is an assistant professor at Laboratory of Biochemistry in Research Faculty of Agriculture, Hokkaido University (Sapporo, Japan). He obtained Ph. D from Graduate School of Agriculture, Hokkaido University in 2006, under the supervision of Professor Atsuo Kimura. He joined the Research Institute of Nihon Shokuhin Kako Co. Ltd. as a researcher (2006-2010), and developed functional oligosaccharides produced from starch. His research interests are structures and functions of carbohydrate active enzymes and efficient synthesis of functional oligosaccharides. He has studied about<br /> <br /> * [[GH1]] rice β-glucosidase <cite>Himeno2013</cite><br /> * [[GH13]] Bacillus sp. AAH-31 α-amylase <cite>Kim2012 Saburi2013</cite><br /> * [[GH13]] Streptococcus mutans dextran glucosidase <cite>Saburi2006 Saburi2007 Hondoh2008 Kobayashi2011 Saburi2013</cite><br /> * [[GH13]] Halomonas sp. H11 α-glucosidase <cite>Ojima2012</cite><br /> * [[GH13]] Bacillus clarkii γ-cyclodextrinase <cite>Nakagawa2008</cite><br /> * [[GH94]] Ruminococcus albus cellobiose phosphorylase <cite>Hamura2012 Hamura2013</cite><br /> * [[GH94]] Ruminococcus albus cellodextrin phosphorylase <cite>Sawano2013</cite><br /> * [[GH130]] Ruminococcus albus 4-O-β-mannosylglucose phosphorylase (RaMP1) <cite>Kawahara2012</cite><br /> * [[GH130]] Rhodothermus marinus 4-O-β-mannosylglucose phosphorylase <cite>Jaito2014</cite><br /> * [[GH130]] Ruminococcus albus β-1,4-mannooligosaccharide phosphorylase (RaMP2) <cite>Kawahara2012</cite><br /> <br /> <br /> <br /> ----<br /> <br /> <biblio><br /> #Himeno2013 pmid=23649259<br /> #>Kim2012 pmid=22785486<br /> #>Saburi2013 pmid=24018662<br /> #>Saburi2006 pmid=16503208<br /> #>Saburi2007 pmid=17768352<br /> <br /> #>Hondoh2008 pmid=18395742<br /> <br /> #>Kobayashi2011 pmid=21821929<br /> #>Saburi2013 pmid=24052257<br /> #>Ojima2012 pmid=22226947<br /> #>Nakagawa2008 pmid=18824139<br /> <br /> #>Hamura2012 pmid=22484959<br /> <br /> #>Hamura2013 pmid=23845516<br /> #>Sawano2013 pmid=23802549<br /> #>Kawahara2012 pmid=23093406<br /> #>Jaito2014 pmid=25036679<br /> <br /> <br /> <br /> </biblio><br /> <br /> <br /> [[Category:Contributors|Lastname,Firstname]]<br /> </div>

Wataru Saburi https://www.cazypedia.org/index.php?title=User_talk:Wataru_Saburi&diff=10323 User talk:Wataru Saburi 2014-10-13T13:41:59Z

<p>Wataru Saburi: </p> <hr /> <div><br /> <br /> [[Image:Saburi2.jpg]]<br /> <br /> '''Wataru Saburi''' is an assistant professor at Laboratory of Biochemistry in Research Faculty of Agriculture, Hokkaido University (Sapporo, Japan). He obtained Ph. D from Graduate School of Agriculture, Hokkaido University in 2006, under the supervision of Professor Atsuo Kimura. He joined the Research Institute of Nihon Shokuhin Kako Co. Ltd. as a researcher (2006-2010), and developed functional oligosaccharides produced from starch. His research interests are structure and function of carbohydrate active enzymes and efficient synthesis of functional oligosaccharides. He has studied about<br /> <br /> * [[GH1]] rice β-glucosidase <cite>Himeno2013</cite><br /> * [[GH13]] Bacillus sp. AAH-31 α-amylase <cite>Kim2012 Saburi2013</cite><br /> * [[GH13]] Streptococcus mutans dextran glucosidase <cite>Saburi2006 Saburi2007 Hondoh2008 Kobayashi2011 Saburi2013</cite><br /> * [[GH13]] Halomonas sp. H11 α-glucosidase <cite>Ojima2012</cite><br /> * [[GH13]] Bacillus clarkii γ-cyclodextrinase <cite>Nakagawa2008</cite><br /> * [[GH94]] Ruminococcus albus cellobiose phosphorylase <cite>Hamura2012 Hamura2013</cite><br /> * [[GH94]] Ruminococcus albus cellodextrin phosphorylase <cite>Sawano2013</cite><br /> * [[GH130]] Ruminococcus albus 4-O-β-mannosylglucose phosphorylase (RaMP1) <cite>Kawahara2012</cite><br /> * [[GH130]] Rhodothermus marinus 4-O-β-mannosylglucose phosphorylase <cite>Jaito2014</cite><br /> * [[GH130]] Ruminococcus albus β-1,4-mannooligosaccharide phosphorylase (RaMP2) <cite>Kawahara2012</cite><br /> <br /> <br /> <br /> ----<br /> <br /> <biblio><br /> #Himeno2013 pmid=23649259<br /> #>Kim2012 pmid=22785486<br /> #>Saburi2013 pmid=24018662<br /> #>Saburi2006 pmid=16503208<br /> #>Saburi2007 pmid=17768352<br /> <br /> #>Hondoh2008 pmid=18395742<br /> <br /> #>Kobayashi2011 pmid=21821929<br /> #>Saburi2013 pmid=24052257<br /> #>Ojima2012 pmid=22226947<br /> #>Nakagawa2008 pmid=18824139<br /> <br /> #>Hamura2012 pmid=22484959<br /> <br /> #>Hamura2013 pmid=23845516<br /> #>Sawano2013 pmid=23802549<br /> #>Kawahara2012 pmid=23093406<br /> #>Jaito2014 pmid=25036679<br /> <br /> <br /> <br /> </biblio><br /> <br /> <br /> [[Category:Contributors|Lastname,Firstname]]<br /> </div>

Wataru Saburi https://www.cazypedia.org/index.php?title=File:Saburi2.jpg&diff=10322 File:Saburi2.jpg 2014-10-13T13:39:11Z

<p>Wataru Saburi: </p> <hr /> <div></div>

Wataru Saburi https://www.cazypedia.org/index.php?title=User_talk:Wataru_Saburi&diff=10321 User talk:Wataru Saburi 2014-10-13T13:19:17Z

<p>Wataru Saburi: Created page with " right '''Wataru Saburi''' is an assistant professor at Laboratory of Biochemistry in Research Faculty of Agriculture, Hokkaido Universi..."</p> <hr /> <div><br /> <br /> [[Image:Blank_user-200px.png|200px|right]]<br /> <br /> '''Wataru Saburi''' is an assistant professor at Laboratory of Biochemistry in Research Faculty of Agriculture, Hokkaido University (Sapporo, Japan). He obtained Ph. D from Graduate School of Agriculture, Hokkaido University in 2006, under the supervision of Professor Atsuo Kimura. He joined the Research Institute of Nihon Shokuhin Kako Co. Ltd. as a researcher (2006-2010), and developed functional oligosaccharides produced from starch. His research interests are structure and function of carbohydrate active enzymes and efficient synthesis of functional oligosaccharides. He has studied about<br /> <br /> * [[GH1]] rice β-glucosidase <cite>Himeno2013</cite><br /> * [[GH13]] Bacillus sp. AAH-31 α-amylase <cite>Kim2012 Saburi2013</cite><br /> * [[GH13]] Streptococcus mutans dextran glucosidase <cite>Saburi2006 Saburi2007 Hondoh2008 Kobayashi2011 Saburi2013</cite><br /> * [[GH13]] Halomonas sp. H11 α-glucosidase <cite>Ojima2012</cite><br /> * [[GH13]] Bacillus clarkii γ-cyclodextrinase <cite>Nakagawa2008</cite><br /> * [[GH94]] Ruminococcus albus cellobiose phosphorylase <cite>Hamura2012 Hamura2013</cite><br /> * [[GH94]] Ruminococcus albus cellodextrin phosphorylase <cite>Sawano2013</cite><br /> * [[GH130]] Ruminococcus albus 4-O-β-mannosylglucose phosphorylase (RaMP1) <cite>Kawahara2012</cite><br /> * [[GH130]] Rhodothermus marinus 4-O-β-mannosylglucose phosphorylase <cite>Jaito2014</cite><br /> * [[GH130]] Ruminococcus albus β-1,4-mannooligosaccharide phosphorylase (RaMP2) <cite>Kawahara2012</cite><br /> * Please upload a picture of yourself using the "Upload file" link in the Toolbox section of the left menu, and then replace the Image filename with your own.<br /> <br /> <br /> <br /> <br /> ----<br /> <br /> <biblio><br /> #Himeno2013 pmid=23649259<br /> #>Kim2012 pmid=22785486<br /> #>Saburi2013 pmid=24018662<br /> #>Saburi2006 pmid=16503208<br /> #>Saburi2007 pmid=17768352<br /> <br /> #>Hondoh2008 pmid=18395742<br /> <br /> #>Kobayashi2011 pmid=21821929<br /> #>Saburi2013 pmid=24052257<br /> #>Ojima2012 pmid=22226947<br /> #>Nakagawa2008 pmid=18824139<br /> <br /> #>Hamura2012 pmid=22484959<br /> <br /> #>Hamura2013 pmid=23845516<br /> #>Sawano2013 pmid=23802549<br /> #>Kawahara2012 pmid=23093406<br /> #>Jaito2014 pmid=25036679<br /> <br /> <br /> <br /> </biblio><br /> <br /> <br /> [[Category:Contributors|Lastname,Firstname]]<br /> </div>

Wataru Saburi