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https://www.cazypedia.org/api.php?action=feedcontributions&feedformat=atom&user=Yuval+Shoham CAZypedia - User contributions [en-ca] 2026-05-04T04:03:49Z User contributions MediaWiki 1.35.10 https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_51&diff=4679 Glycoside Hydrolase Family 51 2010-05-12T15:21:29Z

<p>Yuval Shoham: </p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Yuval Shoham^^^<br /> * [[Responsible Curator]]: ^^^Yuval Shoham^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH51'''<br /> |-<br /> |'''Clan''' <br /> |GH-A<br /> |-<br /> |'''Mechanism'''<br /> |retaining<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |http://www.cazy.org/fam/GH51.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> The majority of the enzymes from this family hydrolyze the glycosidic bond between L-arabinofuranosides side chains of hemicelluloses such as arabinoxylan, arabinogalactan, and L-arabinan. A few enzymes of the family exhibit β 1-4 endoglucanase activity towards carboxy methyl cellulose and xylan <cite>Eckert2003</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Family GH51 L-arabinfuranosidases are [[retaining]] enzymes and follow a classical Koshland double-displacement mechanism. Due to the fast mutarotation and tautomerization rates of arabinose, the stereochemical course of the reaction was determined in presence of methanol and followed by NMR spectroscopy <cite>Pitson1996 Debeche2002 Shallom2002a</cite>. Enzymes that have been well studied kinetically include the ''Geobacillus stearothermophilus'' T-6 and ''Thermobacillus xylanilyticus'' α-L-arabinofuranosidases, for which a detailed kinetic study was performed including kinetics with aryl-α-L-arabinofuranosides bearing various leaving groups, Brønsted plots for the E175A acid-base catalytic residue and azide-rescue for the E294A nucleophilc mutant <cite>Shallom2002b Debeche2002 Shallom2002a</cite>.<br /> <br /> == Catalytic Residues ==<br /> The catalytic acid-base was first identified in ''Thermobacillus xylanilyticus'' (Glu176) <cite>Debeche2002</cite> and in ''Geobacillus stearothermophilus'' T-6 (Glu175) α-arabinofuranosidases <cite>Shallom2002a</cite> using kinetic analysis, pH dependence profiles, and azide rescue of the catalytic mutant. The catalytic nucleophile was first identified in ''Geobacillus stearothermophilus'' α-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensional structures for GH51 arabinofuranosidases are available for ''Geobacillus stearothermophilus'' <cite>Hovel2003</cite> ''[http://www.cazy.org/b514.html Clostridium thermocellum]'' <cite>Taylor2006</cite> and ''Thermobacillus xylanilyticus'' <cite>Paes2008</cite>. The enzyme in solution is a hexamer (can be described as a trimer of dimmers) and each monomer is organized into two domains: a ‘clan GH-A’ catalytic (β/α)<sub>8</sub> domain and a 12-stranded β sandwich with a jelly-roll topology.<br /> <br /> == Family Firsts ==<br /> ;First sterochemistry determination: ''[http://www.cazy.org/e535.html Aspergillus niger]'' and ''Aspergillus aculeatus'' α-L-arabinfuranosidases carried out in the presence of 2.5 M methanol and followed by <sup>1</sup>H-NMR spectroscopy <cite>Pitson1996</cite>.<br /> ;First catalytic nucleophile identification: ''Geobacillus stearothermophilus'' α-L-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue <cite>Shallom2002b</cite>.<br /> ;First general acid/base residue identification: ''Thermobacillus xylanilyticus'' and ''Geobacillus stearothermophilus'' T-6 α-L-arabinofuranosidases ''via'' detailed kinetic studies for the catalytic mutant including azide rescue <cite>Debeche2002 Shallom2002a</cite>.<br /> ;First 3-D structure: ''Geobacillus stearothermophilus'' α-L-arabinofuranosidase <cite>Hovel2003</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Eckert2003 pmid=12919323<br /> #Pitson1996 pmid=8946944<br /> #Debeche2002 pmid=11842234<br /> #Shallom2002a pmid=11943144<br /> #Shallom2002b pmid=12221104<br /> #Hovel2003 pmid=14517232<br /> #Taylor2006 pmid=16336192 <br /> #Paes2008 pmid=18563919 <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH051]]</div>

Yuval Shoham https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_51&diff=4678 Glycoside Hydrolase Family 51 2010-05-12T15:19:52Z

<p>Yuval Shoham: </p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Yuval Shoham^^^<br /> * [[Responsible Curator]]: ^^^Yuval Shoham^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH51'''<br /> |-<br /> |'''Clan''' <br /> |GH-A<br /> |-<br /> |'''Mechanism'''<br /> |retaining<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |http://www.cazy.org/fam/GH51.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> The majority of the enzymes from this family hydrolyze the glycosidic bond between L-arabinofuranosides side chains of hemicelluloses such as arabinoxylan, arabinogalactan, and L-arabinan. A few enzymes of the family exhibit β 1-4 endoglucanase activity towards carboxy methyl cellulose and xylan <cite>Eckert2003</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Family GH51 L-arabinfuranosidases are [[retaining]] enzymes and follow a classical Koshland double-displacement mechanism. Due to the fast mutarotation and tautomerization rates of arabinose, the stereochemical course of the reaction was determined in presence of methanol and followed by NMR spectroscopy <cite>Pitson1996 Debeche2002 Shallom2002a</cite>. Enzymes that have been well studied kinetically include the ''Geobacillus stearothermophilus'' T-6 and ''Thermobacillus xylanilyticus'' α-L-arabinofuranosidases, for which a detailed kinetic study was performed including kinetics with aryl-α-L-arabinofuranosides bearing various leaving groups, Brønsted plots for the E175A acid-base catalytic residue and azide-rescue for the E294A nucleophilc mutant <cite>Shallom2002b Debeche2002 Shallom2002a</cite>.<br /> <br /> == Catalytic Residues ==<br /> The catalytic acid-base was first identified in ''Thermobacillus xylanilyticus'' (Glu176) <cite>Debeche2002</cite> and in ''Geobacillus stearothermophilus'' T-6 (Glu175) α-arabinofuranosidases <cite>Shallom2002a</cite> using kinetic analysis, pH dependence profiles, and azide rescue of the catalytic mutant. The catalytic nucleophile was first identified in ''Geobacillus stearothermophilus'' α-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensional structures for GH51 arabinofuranosidases are available for ''Geobacillus stearothermophilus'' <cite>Hovel2003</cite> ''[http://www.cazy.org/b514.html Clostridium thermocellum]'' <cite>Taylor2006</cite> and ''Thermobacillus xylanilyticus'' <cite>Paes2008</cite>. The enzyme in solution is a hexamer (can be described as a trimer of dimmers) and each monomer is organized into two domains: a ‘clan GH-A’ catalytic (β/α)<sub>8</sub> domain and a 12-stranded β sandwich with a jelly-roll topology.<br /> <gallery widths=200px heights=220px perrow=2 caption="3D structures of GH51 proteins (click images for large versions)"><br /> File:1QW8.jpg|PDB ID [{{PDBlink}}1qw8 1qw8] from "Crystal structure of the α-L-arabinofuranosidase AbfA from ''G. stearothermophilus'' in complex with Ara-α(1,3)-Xyl <cite>Hovel2003</cite>. <br /> </gallery><br /> <br /> <br /> == Family Firsts ==<br /> ;First sterochemistry determination: ''[http://www.cazy.org/e535.html Aspergillus niger]'' and ''Aspergillus aculeatus'' α-L-arabinfuranosidases carried out in the presence of 2.5 M methanol and followed by <sup>1</sup>H-NMR spectroscopy <cite>Pitson1996</cite>.<br /> ;First catalytic nucleophile identification: ''Geobacillus stearothermophilus'' α-L-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue <cite>Shallom2002b</cite>.<br /> ;First general acid/base residue identification: ''Thermobacillus xylanilyticus'' and ''Geobacillus stearothermophilus'' T-6 α-L-arabinofuranosidases ''via'' detailed kinetic studies for the catalytic mutant including azide rescue <cite>Debeche2002 Shallom2002a</cite>.<br /> ;First 3-D structure: ''Geobacillus stearothermophilus'' α-L-arabinofuranosidase <cite>Hovel2003</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Eckert2003 pmid=12919323<br /> #Pitson1996 pmid=8946944<br /> #Debeche2002 pmid=11842234<br /> #Shallom2002a pmid=11943144<br /> #Shallom2002b pmid=12221104<br /> #Hovel2003 pmid=14517232<br /> #Taylor2006 pmid=16336192 <br /> #Paes2008 pmid=18563919 <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH051]]</div>

Yuval Shoham https://www.cazypedia.org/index.php?title=User:Yuval_Shoham&diff=4664 User:Yuval Shoham 2010-05-10T20:27:54Z

<p>Yuval Shoham: </p> <hr /> <div>Yuval Shoham is a Professor of Biotechnology at the Technion-Israel Institute of Technology. He obtained his B.Sc. and M.Sc. in Biology and Microbiology from Tel Aviv University and his PhD in Biochemical Engineering from M.I.T under the supervision of Arnold Demain. In 1988 he joined the Technion and his research focuses on: a) the catalytic mechanisms and structure-function relationships of industrial enzymes especially glycoside hydrolases, and b) gene regulation of the hemicellulolytic and cellulolytic systems in ''Geobacillus stearothermophilus'' and ''Clostridium thermocellum''. He was involved in solving the crystal structures of:<br /> <br /> * ''C. thermocellum'' cellulosomal CBD <cite>Tormo1996</cite> <br /> * ''C. thermocellum'' cohesin domain <cite>Shimon1997</cite><br /> * ''G. stearothermophilus'' [[GH51]] α-L-arabinofuranosidase <cite>Hovel2003</cite><br /> * ''G. stearothermophilus'' [[GH67]] α-glucuronidase <cite>Golan2004</cite><br /> * ''G. stearothermophilus'' [[GH10]] β-xylanase <cite>Teplitsky2004</cite><br /> * ''G. stearothermophilus'' [[GH39]] β-xylosidase <cite>Czjzek2005</cite><br /> * ''G. stearothermophilus'' [[GH43]] β-xylosidase <cite>Brux2006</cite><br /> * ''G. stearothermophilus'' [[GH43]] 1,5-α-L-arabinanase <cite>Alhassid2009</cite><br /> <br /> <br /> ----<br /> <biblio><br /> #Tormo1996 pmid=8918451<br /> #Shimon1997 pmid=9083107<br /> #Hovel2003 pmid=14517232<br /> #Golan2004 pmid=14573597<br /> #Teplitsky2004 pmid=15103129<br /> #Czjzek2005 pmid=16212978<br /> #Brux2006 pmid=16631196 <br /> #Alhassid2009 pmid=19505290 <br /> </biblio><br /> <br /> <br /> [[Category:Contributors|Shoham, Yuval]]</div>

Yuval Shoham https://www.cazypedia.org/index.php?title=User:Yuval_Shoham&diff=4663 User:Yuval Shoham 2010-05-10T20:18:04Z

<p>Yuval Shoham: </p> <hr /> <div>Yuval Shoham is a Professor of Biotechnology at the Technion-Israel Institute of Technology. He obtained his B.Sc. and M.Sc. in Biology and Microbiology from Tel Aviv University and his PhD in Biochemical Engineering from M.I.T under the supervision of Arnold Demain. In 1988 he joined the Technion and his research focuses on: a) the catalytic mechanisms and structure-function relationships of industrial enzymes especially glycoside hydrolases, and b) gene regulation of the hemicellulolytic and cellulolytic systems in ''Geobacillus stearothermophilus'' and ''Clostridium thermocellum''. He was involved in solving the crystal structures of:<br /> <br /> * ''C. thermocellum'' cellulosomal CBD <cite>Tormo1996</cite> <br /> * ''C. thermocellum'' cohesin domain <cite>Shimon1997</cite><br /> * ''G. stearothermophilus'' [[GH51]] α-L-arabinofuranosidase <cite>Hövel2003</cite><br /> * ''G. stearothermophilus'' [[GH67]] α-glucuronidase <cite>Golan2004</cite><br /> * ''G. stearothermophilus'' [[GH10]] β-xylanase <cite>Teplitsky2004</cite><br /> * ''G. stearothermophilus'' [[GH39]] β-xylosidase <cite>Czjzek2005</cite><br /> * ''G. stearothermophilus'' [[GH43]] β-xylosidase <cite>Brüx2006</cite><br /> * ''G. stearothermophilus'' [[GH43]] 1,5-α-L-arabinanase <cite>Alhassid2009</cite><br /> <br /> <br /> ----<br /> <biblio><br /> #Tormo1996 pmid=8918451<br /> #Shimon1997 pmid=9083107<br /> #Hövel2003 pmid=14517232<br /> #Golan2004 pmid=14573597<br /> #Teplitsky2004 pmid=15103129<br /> #Czjzek2005 pmid=16212978<br /> #Brüx2006 pmid=16631196 <br /> #Alhassid2009 pmid=19505290 <br /> </biblio><br /> <br /> <br /> [[Category:Contributors|Shoham, Yuval]]</div>

Yuval Shoham https://www.cazypedia.org/index.php?title=User:Yuval_Shoham&diff=4662 User:Yuval Shoham 2010-05-10T19:20:55Z

<p>Yuval Shoham: </p> <hr /> <div>Yuval Shoham is a Professor of Biotechnology at the Technion-Israel Institute of Technology. He obtained his B.Sc. and M.Sc. in Biology and Microbiology from Tel Aviv University and his PhD in Biochemical Engineering from M.I.T under the supervision of Arnold Demain. In 1988 he joined the Technion and his research focuses on: a) the catalytic mechanisms and structure-function relationships of industrial enzymes especially glycoside hydrolases, and b) gene regulation of the hemicellulolytic and cellulolytic systems in ''Geobacillus stearothermophilus'' and ''Clostridium thermocellum''. He was involved in solving the crystal structures of:<br /> <br /> * ''C. thermocellum'' cellulosomal CBD <br /> * ''C. thermocellum'' cohesin domain <br /> * ''G. stearothermophilus'' [[GH51]] α-L-arabinofuranosidase <br /> * ''G. stearothermophilus'' [[GH67]] α-glucuronidase [4]<br /> * ''G. stearothermophilus'' [[GH10]] β-xylanase [5]<br /> * ''G. stearothermophilus'' [[GH39]] β-xylosidase [6]<br /> * ''G. stearothermophilus'' [[GH43]] β-xylosidase [7]<br /> * ''G. stearothermophilus'' [[GH43]] 1,5-α-L-arabinanase [8]<br /> <br /> <br /> [[Category:Contributors|Shoham, Yuval]]</div>

Yuval Shoham https://www.cazypedia.org/index.php?title=User:Yuval_Shoham&diff=4661 User:Yuval Shoham 2010-05-10T19:19:19Z

<p>Yuval Shoham: </p> <hr /> <div>Yuval Shoham is a Professor of Biotechnology at the Technion-Israel Institute of Technology. He obtained his B.Sc. and M.Sc. in Biology and Microbiology from Tel Aviv University and his PhD in Biochemical Engineering from M.I.T under the supervision of Arnold Demain. In 1988 he joined the Technion and his research focuses on: a) the catalytic mechanisms and structure-function relationships of industrial enzymes especially glycoside hydrolases, and b) gene regulation of the hemicellulolytic and cellulolytic systems in ''Geobacillus stearothermophilus'' and ''Clostridium thermocellum''. He was involved in solving the crystal structures of:<br /> <br /> * ''C. thermocellum'' cellulosomal CBD <br /> * ''C. thermocellum'' cohesin domain <br /> * ''G. stearothermophilus'' [[GH51]] α-L-arabinofuranosidase <br /> * ''G. stearothermophilus'' [[GH67]] α-glucuronidase [4]<br /> * ''G. stearothermophilus'' [[GH10]] -xylanase [5]<br /> * ''G. stearothermophilus'' [[GH39]]  -xylosidase [6]<br /> * ''G. stearothermophilus'' [[GH43]]  -xylosidase [7]<br /> * ''G. stearothermophilus'' [[GH43]] 1,5-α-L-arabinanase [8]<br /> <br /> <br /> [[Category:Contributors|Shoham, Yuval]]</div>

Yuval Shoham https://www.cazypedia.org/index.php?title=User:Yuval_Shoham&diff=4660 User:Yuval Shoham 2010-05-10T19:18:32Z

<p>Yuval Shoham: </p> <hr /> <div>Yuval Shoham is a Professor of Biotechnology at the Technion-Israel Institute of Technology. He obtained his B.Sc. and M.Sc. in Biology and Microbiology from Tel Aviv University and his PhD in Biochemical Engineering from M.I.T under the supervision of Arnold Demain. In 1988 he joined the Technion and his research focuses on: a) the catalytic mechanisms and structure-function relationships of industrial enzymes especially glycoside hydrolases, and b) gene regulation of the hemicellulolytic and cellulolytic systems in ''Geobacillus stearothermophilus'' and ''Clostridium thermocellum''. He was involved in solving the crystal structures of:<br /> <br /> * ''C. thermocellum'' cellulosomal CBD <br /> * ''C. thermocellum'' cohesin domain <br /> * ''G. stearothermophilus'' [[GH51]] α-L-arabinofuranosidase <br /> * ''G. stearothermophilus'' GH67 α-glucuronidase [4]<br /> * ''G. stearothermophilus'' GH10 -xylanase [5]<br /> * ''G. stearothermophilus'' GH39  -xylosidase [6]<br /> * ''G. stearothermophilus'' GH43  -xylosidase [7]<br /> * ''G. stearothermophilus'' GH43 1,5-α-L-arabinanase [8]<br /> <br /> <br /> [[Category:Contributors|Shoham, Yuval]]</div>

Yuval Shoham https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_51&diff=4659 Glycoside Hydrolase Family 51 2010-05-10T17:37:57Z

<p>Yuval Shoham: /* Kinetics and Mechanism */</p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Yuval Shoham^^^<br /> * [[Responsible Curator]]: ^^^Yuval Shoham^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH51'''<br /> |-<br /> |'''Clan''' <br /> |GH-A<br /> |-<br /> |'''Mechanism'''<br /> |retaining<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |http://www.cazy.org/fam/GH51.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> The majority of the enzymes from this family hydrolyze the glycosidic bond between L-arabinofuranosides side chains of hemicelluloses such as arabinoxylan, arabinogalactan, and L-arabinan. A few enzymes of the family exhibit β 1-4 endoglucanase activity towards carboxy methyl cellulose and xylan <cite>Eckert2003</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Family GH51 L-arabinfuranosidases are [[retaining]] enzymes and follow a classical Koshland double-displacement mechanism. Due to the fast mutarotation and tautomerization rates of arabinose, the stereochemical course of the reaction was determined in presence of methanol and followed by NMR spectroscopy <cite>Pitson1996 Debeche2002 Shallom2002a</cite>. Enzymes that have been well studied kinetically include the ''Geobacillus stearothermophilus'' T-6 and ''Thermobacillus xylanilyticus'' α-L-arabinofuranosidases, for which a detailed kinetic study was performed including kinetics with aryl-α-L-arabinofuranosides bearing various leaving groups, Brønsted plots for the E175A acid-base catalytic residue and azide-rescue for the E294A nucleophilc mutant <cite>Shallom2002b Debeche2002 Shallom2002a</cite>.<br /> <br /> == Catalytic Residues ==<br /> The catalytic acid-base was first identified in ''Thermobacillus xylanilyticus'' (Glu176) <cite>Debeche2002</cite> and in ''Geobacillus stearothermophilus'' T-6 (Glu175) α-arabinofuranosidases <cite>Shallom2002a</cite> using kinetic analysis, pH dependence profiles, and azide rescue of the catalytic mutant. The catalytic nucleophile was first identified in ''Geobacillus stearothermophilus'' α-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensional structures for GH51 arabinofuranosidases are available for ''Geobacillus stearothermophilus'' <cite>Hovel2003</cite> ''[http://www.cazy.org/b514.html Clostridium thermocellum]'' <cite>Taylor2006</cite> and ''Thermobacillus xylanilyticus'' <cite>Paes2008</cite>. The enzyme in solution is a hexamer (can be described as a trimer of dimmers) and each monomer is organized into two domains: a ‘clan GH-A’ catalytic (β/α)<sub>8</sub> domain and a 12-stranded β sandwich with a jelly-roll topology.<br /> <br /> == Family Firsts ==<br /> ;First sterochemistry determination: ''[http://www.cazy.org/e535.html Aspergillus niger]'' and ''Aspergillus aculeatus'' α-L-arabinfuranosidases carried out in the presence of 2.5 M methanol and followed by <sup>1</sup>H-NMR spectroscopy <cite>Pitson1996</cite>.<br /> ;First catalytic nucleophile identification: ''Geobacillus stearothermophilus'' α-L-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue <cite>Shallom2002b</cite>.<br /> ;First general acid/base residue identification: ''Thermobacillus xylanilyticus'' and ''Geobacillus stearothermophilus'' T-6 α-L-arabinofuranosidases ''via'' detailed kinetic studies for the catalytic mutant including azide rescue <cite>Debeche2002 Shallom2002a</cite>.<br /> ;First 3-D structure: ''Geobacillus stearothermophilus'' α-L-arabinofuranosidase <cite>Hovel2003</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Eckert2003 pmid=12919323<br /> #Pitson1996 pmid=8946944<br /> #Debeche2002 pmid=11842234<br /> #Shallom2002a pmid=11943144<br /> #Shallom2002b pmid=12221104<br /> #Hovel2003 pmid=14517232<br /> #Taylor2006 pmid=16336192 <br /> #Paes2008 pmid=18563919 <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH051]]</div>

Yuval Shoham https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_51&diff=4658 Glycoside Hydrolase Family 51 2010-05-10T17:35:53Z

<p>Yuval Shoham: /* Family Firsts */</p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Yuval Shoham^^^<br /> * [[Responsible Curator]]: ^^^Yuval Shoham^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH51'''<br /> |-<br /> |'''Clan''' <br /> |GH-A<br /> |-<br /> |'''Mechanism'''<br /> |retaining<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |http://www.cazy.org/fam/GH51.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> The majority of the enzymes from this family hydrolyze the glycosidic bond between L-arabinofuranosides side chains of hemicelluloses such as arabinoxylan, arabinogalactan, and L-arabinan. A few enzymes of the family exhibit β 1-4 endoglucanase activity towards carboxy methyl cellulose and xylan <cite>Eckert2003</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Family GH51 L-arabinfuranosidases are retaining enzymes and follow a classical Koshland double-displacement mechanism. Due to the fast mutarotation and tautomerization rates of arabinose, the stereochemical course of the reaction was determined in presence of methanol and followed by NMR spectroscopy <cite>Pitson1996 Debeche2002 Shallom2002a</cite>. Enzymes that have been well studied kinetically include the ''Geobacillus stearothermophilus'' T-6 and ''Thermobacillus xylanilyticus'' α-L-arabinofuranosidases, for which a detailed kinetic study was performed including kinetics with aryl-α-L-arabinofuranosides bearing various leaving groups, Brønsted plots for the E175A acid-base catalytic residue and azide-rescue for the E294A nucleophilc mutant <cite>Shallom2002b Debeche2002 Shallom2002a</cite>.<br /> <br /> == Catalytic Residues ==<br /> The catalytic acid-base was first identified in ''Thermobacillus xylanilyticus'' (Glu176) <cite>Debeche2002</cite> and in ''Geobacillus stearothermophilus'' T-6 (Glu175) α-arabinofuranosidases <cite>Shallom2002a</cite> using kinetic analysis, pH dependence profiles, and azide rescue of the catalytic mutant. The catalytic nucleophile was first identified in ''Geobacillus stearothermophilus'' α-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensional structures for GH51 arabinofuranosidases are available for ''Geobacillus stearothermophilus'' <cite>Hovel2003</cite> ''[http://www.cazy.org/b514.html Clostridium thermocellum]'' <cite>Taylor2006</cite> and ''Thermobacillus xylanilyticus'' <cite>Paes2008</cite>. The enzyme in solution is a hexamer (can be described as a trimer of dimmers) and each monomer is organized into two domains: a ‘clan GH-A’ catalytic (β/α)<sub>8</sub> domain and a 12-stranded β sandwich with a jelly-roll topology.<br /> <br /> == Family Firsts ==<br /> ;First sterochemistry determination: ''[http://www.cazy.org/e535.html Aspergillus niger]'' and ''Aspergillus aculeatus'' α-L-arabinfuranosidases carried out in the presence of 2.5 M methanol and followed by <sup>1</sup>H-NMR spectroscopy <cite>Pitson1996</cite>.<br /> ;First catalytic nucleophile identification: ''Geobacillus stearothermophilus'' α-L-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue <cite>Shallom2002b</cite>.<br /> ;First general acid/base residue identification: ''Thermobacillus xylanilyticus'' and ''Geobacillus stearothermophilus'' T-6 α-L-arabinofuranosidases ''via'' detailed kinetic studies for the catalytic mutant including azide rescue <cite>Debeche2002 Shallom2002a</cite>.<br /> ;First 3-D structure: ''Geobacillus stearothermophilus'' α-L-arabinofuranosidase <cite>Hovel2003</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Eckert2003 pmid=12919323<br /> #Pitson1996 pmid=8946944<br /> #Debeche2002 pmid=11842234<br /> #Shallom2002a pmid=11943144<br /> #Shallom2002b pmid=12221104<br /> #Hovel2003 pmid=14517232<br /> #Taylor2006 pmid=16336192 <br /> #Paes2008 pmid=18563919 <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH051]]</div>

Yuval Shoham https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_51&diff=4657 Glycoside Hydrolase Family 51 2010-05-10T17:31:35Z

<p>Yuval Shoham: /* Three-dimensional structures */</p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Yuval Shoham^^^<br /> * [[Responsible Curator]]: ^^^Yuval Shoham^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH51'''<br /> |-<br /> |'''Clan''' <br /> |GH-A<br /> |-<br /> |'''Mechanism'''<br /> |retaining<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |http://www.cazy.org/fam/GH51.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> The majority of the enzymes from this family hydrolyze the glycosidic bond between L-arabinofuranosides side chains of hemicelluloses such as arabinoxylan, arabinogalactan, and L-arabinan. A few enzymes of the family exhibit β 1-4 endoglucanase activity towards carboxy methyl cellulose and xylan <cite>Eckert2003</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Family GH51 L-arabinfuranosidases are retaining enzymes and follow a classical Koshland double-displacement mechanism. Due to the fast mutarotation and tautomerization rates of arabinose, the stereochemical course of the reaction was determined in presence of methanol and followed by NMR spectroscopy <cite>Pitson1996 Debeche2002 Shallom2002a</cite>. Enzymes that have been well studied kinetically include the ''Geobacillus stearothermophilus'' T-6 and ''Thermobacillus xylanilyticus'' α-L-arabinofuranosidases, for which a detailed kinetic study was performed including kinetics with aryl-α-L-arabinofuranosides bearing various leaving groups, Brønsted plots for the E175A acid-base catalytic residue and azide-rescue for the E294A nucleophilc mutant <cite>Shallom2002b Debeche2002 Shallom2002a</cite>.<br /> <br /> == Catalytic Residues ==<br /> The catalytic acid-base was first identified in ''Thermobacillus xylanilyticus'' (Glu176) <cite>Debeche2002</cite> and in ''Geobacillus stearothermophilus'' T-6 (Glu175) α-arabinofuranosidases <cite>Shallom2002a</cite> using kinetic analysis, pH dependence profiles, and azide rescue of the catalytic mutant. The catalytic nucleophile was first identified in ''Geobacillus stearothermophilus'' α-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensional structures for GH51 arabinofuranosidases are available for ''Geobacillus stearothermophilus'' <cite>Hovel2003</cite> ''[http://www.cazy.org/b514.html Clostridium thermocellum]'' <cite>Taylor2006</cite> and ''Thermobacillus xylanilyticus'' <cite>Paes2008</cite>. The enzyme in solution is a hexamer (can be described as a trimer of dimmers) and each monomer is organized into two domains: a ‘clan GH-A’ catalytic (β/α)<sub>8</sub> domain and a 12-stranded β sandwich with a jelly-roll topology.<br /> <br /> == Family Firsts ==<br /> ;First sterochemistry determination: ''Aspergillus niger'' and ''Aspergillus aculeatus'' α-L-arabinfuranosidases carried out in the presence of 2.5 M methanol and followed by <sup>1</sup>H-NMR spectroscopy <cite>Pitson1996</cite>.<br /> ;First catalytic nucleophile identification: ''Geobacillus stearothermophilus'' α-L-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue <cite>Shallom2002b</cite>.<br /> ;First general acid/base residue identification: ''Thermobacillus xylanilyticus'' and ''Geobacillus stearothermophilus'' T-6 α-L-arabinofuranosidases ''via'' detailed kinetic studies for the catalytic mutant including azide rescue <cite>Debeche2002 Shallom2002a</cite>.<br /> ;First 3-D structure: ''Geobacillus stearothermophilus'' α-L-arabinofuranosidase <cite>Hovel2003</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Eckert2003 pmid=12919323<br /> #Pitson1996 pmid=8946944<br /> #Debeche2002 pmid=11842234<br /> #Shallom2002a pmid=11943144<br /> #Shallom2002b pmid=12221104<br /> #Hovel2003 pmid=14517232<br /> #Taylor2006 pmid=16336192 <br /> #Paes2008 pmid=18563919 <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH051]]</div>

Yuval Shoham https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_51&diff=4656 Glycoside Hydrolase Family 51 2010-05-10T15:16:53Z

<p>Yuval Shoham: </p> <hr /> <div><br /> {{CuratorApproved}}<br /> * [[Author]]: ^^^Yuval Shoham^^^<br /> * [[Responsible Curator]]: ^^^Yuval Shoham^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH51'''<br /> |-<br /> |'''Clan''' <br /> |GH-A<br /> |-<br /> |'''Mechanism'''<br /> |retaining<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |http://www.cazy.org/fam/GH51.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> The majority of the enzymes from this family hydrolyze the glycosidic bond between L-arabinofuranosides side chains of hemicelluloses such as arabinoxylan, arabinogalactan, and L-arabinan. A few enzymes of the family exhibit β 1-4 endoglucanase activity towards carboxy methyl cellulose and xylan <cite>Eckert2003</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Family GH51 L-arabinfuranosidases are retaining enzymes and follow a classical Koshland double-displacement mechanism. Due to the fast mutarotation and tautomerization rates of arabinose, the stereochemical course of the reaction was determined in presence of methanol and followed by NMR spectroscopy <cite>Pitson1996 Debeche2002 Shallom2002a</cite>. Enzymes that have been well studied kinetically include the ''Geobacillus stearothermophilus'' T-6 and ''Thermobacillus xylanilyticus'' α-L-arabinofuranosidases, for which a detailed kinetic study was performed including kinetics with aryl-α-L-arabinofuranosides bearing various leaving groups, Brønsted plots for the E175A acid-base catalytic residue and azide-rescue for the E294A nucleophilc mutant <cite>Shallom2002b Debeche2002 Shallom2002a</cite>.<br /> <br /> == Catalytic Residues ==<br /> The catalytic acid-base was first identified in ''Thermobacillus xylanilyticus'' (Glu176) <cite>Debeche2002</cite> and in ''Geobacillus stearothermophilus'' T-6 (Glu175) α-arabinofuranosidases <cite>Shallom2002a</cite> using kinetic analysis, pH dependence profiles, and azide rescue of the catalytic mutant. The catalytic nucleophile was first identified in ''Geobacillus stearothermophilus'' α-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensional structures for GH51 arabinofuranosidases are available for ''Geobacillus stearothermophilus'' <cite>Hovel2003</cite> ''Clostridium thermocellum'' <cite>Taylor2006</cite> and ''Thermobacillus xylanilyticus'' <cite>Paes2008</cite>. The enzyme in solution is a hexamer (can be described as a trimer of dimmers) and each monomer is organized into two domains: a ‘clan GH-A’ catalytic (β/α)<sub>8</sub> domain and a 12-stranded β sandwich with a jelly-roll topology. <br /> <br /> == Family Firsts ==<br /> ;First sterochemistry determination: ''Aspergillus niger'' and ''Aspergillus aculeatus'' α-L-arabinfuranosidases carried out in the presence of 2.5 M methanol and followed by <sup>1</sup>H-NMR spectroscopy <cite>Pitson1996</cite>.<br /> ;First catalytic nucleophile identification: ''Geobacillus stearothermophilus'' α-L-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue <cite>Shallom2002b</cite>.<br /> ;First general acid/base residue identification: ''Thermobacillus xylanilyticus'' and ''Geobacillus stearothermophilus'' T-6 α-L-arabinofuranosidases ''via'' detailed kinetic studies for the catalytic mutant including azide rescue <cite>Debeche2002 Shallom2002a</cite>.<br /> ;First 3-D structure: ''Geobacillus stearothermophilus'' α-L-arabinofuranosidase <cite>Hovel2003</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Eckert2003 pmid=12919323<br /> #Pitson1996 pmid=8946944<br /> #Debeche2002 pmid=11842234<br /> #Shallom2002a pmid=11943144<br /> #Shallom2002b pmid=12221104<br /> #Hovel2003 pmid=14517232<br /> #Taylor2006 pmid=16336192 <br /> #Paes2008 pmid=18563919 <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH051]]</div>

Yuval Shoham https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_51&diff=4655 Glycoside Hydrolase Family 51 2010-05-10T15:10:03Z

<p>Yuval Shoham: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Yuval Shoham^^^<br /> * [[Responsible Curator]]: ^^^Yuval Shoham^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH51'''<br /> |-<br /> |'''Clan''' <br /> |GH-A<br /> |-<br /> |'''Mechanism'''<br /> |retaining<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |http://www.cazy.org/fam/GH51.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> The majority of the enzymes from this family hydrolyze the glycosidic bond between L-arabinofuranosides side chains of hemicelluloses such as arabinoxylan, arabinogalactan, and L-arabinan. A few enzymes of the family exhibit β 1-4 endoglucanase activity towards carboxy methyl cellulose and xylan <cite>Eckert2003</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Family GH51 L-arabinfuranosidases are retaining enzymes and follow a classical Koshland double-displacement mechanism. Due to the fast mutarotation and tautomerization rates of arabinose, the stereochemical course of the reaction was determined in presence of methanol and followed by NMR spectroscopy <cite>Pitson1996 Debeche2002 Shallom2002a</cite>. Enzymes that have been well studied kinetically include the ''Geobacillus stearothermophilus'' T-6 and ''Thermobacillus xylanilyticus'' α-L-arabinofuranosidases, for which a detailed kinetic study was performed including kinetics with aryl-α-L-arabinofuranosides bearing various leaving groups, Brønsted plots for the E175A acid-base catalytic residue and azide-rescue for the E294A nucleophilc mutant <cite>Shallom2002b Debeche2002 Shallom2002a</cite>.<br /> <br /> == Catalytic Residues ==<br /> The catalytic acid-base was first identified in ''Thermobacillus xylanilyticus'' (Glu176) <cite>Debeche2002</cite> and in ''Geobacillus stearothermophilus'' T-6 (Glu175) α-arabinofuranosidases <cite>Shallom2002a</cite> using kinetic analysis, pH dependence profiles, and azide rescue of the catalytic mutant. The catalytic nucleophile was first identified in ''Geobacillus stearothermophilus'' α-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensional structures for GH51 arabinofuranosidases are available for ''Geobacillus stearothermophilus'' <cite>Hovel2003</cite> ''Clostridium thermocellum'' <cite>Taylor2006</cite> and ''Thermobacillus xylanilyticus'' <cite>Paes2008</cite>. The enzyme in solution is a hexamer (can be described as a trimer of dimmers) and each monomer is organized into two domains: a ‘clan GH-A’ catalytic (β/α)<sub>8</sub> domain and a 12-stranded β sandwich with a jelly-roll topology. <br /> <br /> == Family Firsts ==<br /> ;First sterochemistry determination: ''Aspergillus niger'' and ''Aspergillus aculeatus'' α-L-arabinfuranosidases carried out in the presence of 2.5 M methanol and followed by <sup>1</sup>H-NMR spectroscopy <cite>Pitson1996</cite>.<br /> ;First catalytic nucleophile identification: ''Geobacillus stearothermophilus'' α-L-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue <cite>Shallom2002b</cite>.<br /> ;First general acid/base residue identification: ''Thermobacillus xylanilyticus'' and ''Geobacillus stearothermophilus'' T-6 α-L-arabinofuranosidases ''via'' detailed kinetic studies for the catalytic mutant including azide rescue <cite>Debeche2002 Shallom2002a</cite>.<br /> ;First 3-D structure: ''Geobacillus stearothermophilus'' α-L-arabinofuranosidase <cite>Hovel2003</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Eckert2003 pmid=12919323<br /> #Pitson1996 pmid=8946944<br /> #Debeche2002 pmid=11842234<br /> #Shallom2002a pmid=11943144<br /> #Shallom2002b pmid=12221104<br /> #Hovel2003 pmid=14517232<br /> #Taylor2006 pmid=16336192 <br /> #Paes2008 pmid=18563919 <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH051]]</div>

Yuval Shoham https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_51&diff=4654 Glycoside Hydrolase Family 51 2010-05-10T14:53:06Z

<p>Yuval Shoham: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Yuval Shoham^^^<br /> * [[Responsible Curator]]: ^^^Yuval Shoham^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH51'''<br /> |-<br /> |'''Clan''' <br /> |GH-A<br /> |-<br /> |'''Mechanism'''<br /> |retaining<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |http://www.cazy.org/fam/GH51.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> The majority of the enzymes from this family hydrolyze the glycosidic bond between L-arabinofuranosides side chains of hemicelluloses such as arabinoxylan, arabinogalactan, and L-arabinan. A few enzymes of the family exhibit beta 1-4 endoglucanase activity towards carboxy methyl cellulose and xylan <cite>Eckert2003</cite>. <br /> <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Family GH51 L-arabinfuranosidases are retaining enzymes and follow a classical Koshland double-displacement mechanism. Due to the fast mutarotation and tautomerization rates of arabinose, the stereochemical course of the reaction was determined in presence of methanol and followed by NMR spectroscopy <cite>Pitson1996 Debeche2002 Shallom2002a</cite>. Enzymes that have been well studied kinetically include the ''Geobacillus stearothermophilus'' T-6 and ''Thermobacillus xylanilyticus'' alpha L-arabinofuranosidases, for which a detailed kinetic study was performed including kinetics with aryl-α-L-arabinofuranosides bearing various leaving groups, Brønsted plots for the E175A acid-base catalytic residue and azide-rescue for the E294A nucleophilc mutant <cite>Shallom2002b Debeche2002 Shallom2002a</cite>.<br /> <br /> <br /> == Catalytic Residues ==<br /> The catalytic acid-base was first identified in ''Thermobacillus xylanilyticus'' (Glu176) <cite>Debeche2002</cite> and in ''Geobacillus stearothermophilus'' T-6 (Glu175) alpha-arabinofuranosidases <cite>Shallom2002a</cite> using kinetic analysis, pH dependence profiles, and azide rescue of the catalytic mutant. The catalytic nucleophile was first identified in ''Geobacillus stearothermophilus'' alpha-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue.<br /> <br /> <br /> == Three-dimensional structures ==<br /> Three-dimensional structures for GH51 arabinofuranosidases are available for ''G. stearothermophilus'' <cite>Hovel2003</cite> ''C. thermocellum'' <cite>Taylor2006</cite> and ''Thermobacillus xylanilyticus'' <cite>Paes2008</cite>. The enzyme in solution is a hexamer (can be described as a trimer of dimmers) and each monomer is organized into two domains: a ‘clan GH-A’ catalytic (β/α)8 domain and a 12-stranded beta sandwich with a jelly-roll topology. <br /> <br /> <br /> == Family Firsts ==<br /> ;First sterochemistry determination: ''Aspergillus niger'' and ''Aspergillus aculeatus'' alpha-L-arabinfuranosidases carried out in the presence of 2.5 M methanol and followed by 1H-NMR spectroscopy <cite>Pitson1996</cite>.<br /> ;First catalytic nucleophile identification: ''Geobacillus stearothermophilus'' alpha-L-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue <cite>Shallom2002b</cite>.<br /> ;First general acid/base residue identification: ''Thermobacillus xylanilyticus'' and ''Geobacillus stearothermophilus'' T-6 alpha-L-arabinofuranosidases ''via'' detailed kinetic studies for the catalytic mutant including azide rescue <cite>Debeche2002 Shallom2002a</cite>.<br /> ;First 3-D structure: ''Geobacillus stearothermophilus'' alpha-L-arabinofuranosidase <cite>Hovel2003</cite>.<br /> <br /> <br /> == References ==<br /> <biblio><br /> #Eckert2003 pmid=12919323<br /> #Pitson1996 pmid=8946944<br /> #Debeche2002 pmid=11842234<br /> #Shallom2002a pmid=11943144<br /> #Shallom2002b pmid=12221104<br /> #Hovel2003 pmid=14517232<br /> #Taylor2006 pmid=16336192 <br /> #Paes2008 pmid=18563919 <br /> </biblio><br /> <br /> <br /> <br /> [[Category:Glycoside Hydrolase Families|GH051]]</div>

Yuval Shoham https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_51&diff=4653 Glycoside Hydrolase Family 51 2010-05-10T14:16:52Z

<p>Yuval Shoham: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Yuval Shoham^^^<br /> * [[Responsible Curator]]: ^^^Yuval Shoham^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH51'''<br /> |-<br /> |'''Clan''' <br /> |GH-A<br /> |-<br /> |'''Mechanism'''<br /> |retaining<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |http://www.cazy.org/fam/GH51.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> The majority of the enzymes from this family hydrolyze the glycosidic bond between L-arabinofuranosides side chains of hemicelluloses such as arabinoxylan, arabinogalactan, and L-arabinan. A few enzymes of the family exhibit beta 1-4 endoglucanase activity towards carboxy methyl cellulose and xylan <cite>Eckert2003</cite>. <br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>3</cite>. References that are not in PubMed can be typed in by hand <cite>MikesClassic</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Family GH51 L-arabinfuranosidases are retaining enzymes and follow a classical Koshland double-displacement mechanism. Due to the fast mutarotation and tautomerization rates of arabinose, the stereochemical course of the reaction was determined in presence of methanol and followed by NMR spectroscopy <cite>Pitson1996 Debeche2002 Shallom2002a</cite>. Enzymes that have been well studied kinetically include the ''Geobacillus stearothermophilus'' T-6 and ''Thermobacillus xylanilyticus'' alpha L-arabinofuranosidases, for which a detailed kinetic study was performed including kinetics with aryl-α-L-arabinofuranosides bearing various leaving groups, Brønsted plots for the E175A acid-base catalytic residue and azide-rescue for the E294A nucleophilc mutant <cite>Shallom2002b Debeche2002 Shallom2002a</cite>.<br /> <br /> <br /> == Catalytic Residues ==<br /> The catalytic acid-base was first identified in ''Thermobacillus xylanilyticus'' (Glu176) <cite>Debeche2002</cite> and in ''Geobacillus stearothermophilus'' T-6 (Glu175) alpha-arabinofuranosidases <cite>Shallom2002a</cite> using kinetic analysis, pH dependence profiles, and azide rescue of the catalytic mutant. The catalytic nucleophile was first identified in ''Geobacillus stearothermophilus'' alpha-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensional structures for GH51 arabinofuranosidases are available for ''G. stearothermophilus'' <cite>Hovel2003</cite> ''C. thermocellum'' <cite>Taylor2006</cite> and ''Thermobacillus xylanilyticus'' <cite>Paes2008</cite>. The enzyme in solution is a hexamer (can be described as a trimer of dimmers) and each monomer is organized into two domains: a ‘clan GH-A’ catalytic (β/α)8 domain and a 12-stranded beta sandwich with a jelly-roll topology. <br /> <br /> <br /> == Family Firsts ==<br /> ;First sterochemistry determination: Aspergillus niger and Aspergillus aculeatus alpha-L-arabinfuranosidases carried out in the presence of 2.5 M methanol and followed by 1H-NMR spectroscopy <cite>Pitson1996</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>MikesClassic</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>3</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Eckert2003 pmid=12919323<br /> #Pitson1996 pmid=8946944<br /> #Debeche2002 pmid=11842234<br /> #Shallom2002a pmid=11943144<br /> #Shallom2002b pmid=12221104<br /> #Hovel2003 pmid=14517232<br /> #Taylor2006 pmid=16336192 <br /> #Paes2008 pmid=18563919 <br /> #Comfort2007 pmid=17323919<br /> #He1999 pmid=9312086<br /> #3 isbn=978-0-240-52118-3<br /> #MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH051]]</div>

Yuval Shoham https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_51&diff=4652 Glycoside Hydrolase Family 51 2010-05-10T14:12:16Z

<p>Yuval Shoham: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Yuval Shoham^^^<br /> * [[Responsible Curator]]: ^^^Yuval Shoham^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH51'''<br /> |-<br /> |'''Clan''' <br /> |GH-A<br /> |-<br /> |'''Mechanism'''<br /> |retaining<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |http://www.cazy.org/fam/GH51.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> The majority of the enzymes from this family hydrolyze the glycosidic bond between L-arabinofuranosides side chains of hemicelluloses such as arabinoxylan, arabinogalactan, and L-arabinan. A few enzymes of the family exhibit beta 1-4 endoglucanase activity towards carboxy methyl cellulose and xylan <cite>Eckert2003</cite>. <br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>3</cite>. References that are not in PubMed can be typed in by hand <cite>MikesClassic</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Family GH51 L-arabinfuranosidases are retaining enzymes and follow a classical Koshland double-displacement mechanism. Due to the fast mutarotation and tautomerization rates of arabinose, the stereochemical course of the reaction was determined in presence of methanol and followed by NMR spectroscopy <cite>Pitson1996 Debeche2002 Shallom2002a</cite>. Enzymes that have been well studied kinetically include the ''Geobacillus stearothermophilus'' T-6 and ''Thermobacillus xylanilyticus'' alpha L-arabinofuranosidases, for which a detailed kinetic study was performed including kinetics with aryl-α-L-arabinofuranosides bearing various leaving groups, Brønsted plots for the E175A acid-base catalytic residue and azide-rescue for the E294A nucleophilc mutant <cite>Shallom2002b Debeche2002 Shallom2002a</cite>.<br /> <br /> <br /> == Catalytic Residues ==<br /> The catalytic acid-base was first identified in ''Thermobacillus xylanilyticus'' (Glu176) <cite>Debeche2002</cite> and in ''Geobacillus stearothermophilus'' T-6 (Glu175) alpha-arabinofuranosidases <cite>Shallom2002a</cite> using kinetic analysis, pH dependence profiles, and azide rescue of the catalytic mutant. The catalytic nucleophile was first identified in ''Geobacillus stearothermophilus'' alpha-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue.<br /> <br /> == Three-dimensional structures ==<br /> Three-dimensional structures for GH51 arabinofuranosidases are available for ''G. stearothermophilus'' <cite>Hovel2003</cite> ''C. thermocellum'' <cite>Taylor2006</cite> and ''Thermobacillus xylanilyticus'' <cite>Paes2008</cite>. The enzyme in solution is a hexamer (can be described as a trimer of dimmers) and each monomer is organized into two domains: a ‘clan GH-A’ catalytic (β/α)8 domain and a 12-stranded beta sandwich with a jelly-roll topology. <br /> <br /> <br /> == Family Firsts ==<br /> ;First sterochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>MikesClassic</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>3</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Eckert2003 pmid=12919323<br /> #Pitson1996 pmid=8946944<br /> #Debeche2002 pmid=11842234<br /> #Shallom2002a pmid=11943144<br /> #Shallom2002b pmid=12221104<br /> #Hovel2003 pmid=14517232<br /> #Taylor2006 pmid=16336192 <br /> #Paes2008 pmid=18563919 <br /> #Comfort2007 pmid=17323919<br /> #He1999 pmid=9312086<br /> #3 isbn=978-0-240-52118-3<br /> #MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH051]]</div>

Yuval Shoham https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_51&diff=4651 Glycoside Hydrolase Family 51 2010-05-10T14:00:48Z

<p>Yuval Shoham: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Yuval Shoham^^^<br /> * [[Responsible Curator]]: ^^^Yuval Shoham^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH51'''<br /> |-<br /> |'''Clan''' <br /> |GH-A<br /> |-<br /> |'''Mechanism'''<br /> |retaining<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |http://www.cazy.org/fam/GH51.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> The majority of the enzymes from this family hydrolyze the glycosidic bond between L-arabinofuranosides side chains of hemicelluloses such as arabinoxylan, arabinogalactan, and L-arabinan. A few enzymes of the family exhibit beta 1-4 endoglucanase activity towards carboxy methyl cellulose and xylan <cite>Eckert2003</cite>. <br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>3</cite>. References that are not in PubMed can be typed in by hand <cite>MikesClassic</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Family GH51 L-arabinfuranosidases are retaining enzymes and follow a classical Koshland double-displacement mechanism. Due to the fast mutarotation and tautomerization rates of arabinose, the stereochemical course of the reaction was determined in presence of methanol and followed by NMR spectroscopy <cite>Pitson1996 Debeche2002 Shallom2002a</cite>. Enzymes that have been well studied kinetically include the ''Geobacillus stearothermophilus'' T-6 and ''Thermobacillus xylanilyticus'' alpha L-arabinofuranosidases, for which a detailed kinetic study was performed including kinetics with aryl-α-L-arabinofuranosides bearing various leaving groups, Brønsted plots for the E175A acid-base catalytic residue and azide-rescue for the E294A nucleophilc mutant <cite>Shallom2002b Debeche2002 Shallom2002a</cite>.<br /> <br /> <br /> == Catalytic Residues ==<br /> The catalytic acid-base was first identified in ''Thermobacillus xylanilyticus'' (Glu176) <cite>Debeche2002</cite> and in ''Geobacillus stearothermophilus'' T-6 (Glu175) alpha-arabinofuranosidases <cite>Shallom2002a</cite> using kinetic analysis, pH dependence profiles, and azide rescue of the catalytic mutant. The catalytic nucleophile was first identified in ''Geobacillus stearothermophilus'' alpha-arabinofuranosidase through detailed kinetic studies for the catalytic mutant including azide rescue.<br /> <br /> == Three-dimensional structures ==<br /> Content is to be added here.<br /> <br /> <br /> == Family Firsts ==<br /> ;First sterochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>MikesClassic</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>3</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Eckert2003 pmid=12919323<br /> #Pitson1996 pmid=8946944<br /> #Debeche2002 pmid=11842234<br /> #Shallom2002a pmid=11943144<br /> #Shallom2002b pmid=12221104 <br /> #Comfort2007 pmid=17323919<br /> #He1999 pmid=9312086<br /> #3 isbn=978-0-240-52118-3<br /> #MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH051]]</div>

Yuval Shoham https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_51&diff=4650 Glycoside Hydrolase Family 51 2010-05-10T13:54:46Z

<p>Yuval Shoham: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Yuval Shoham^^^<br /> * [[Responsible Curator]]: ^^^Yuval Shoham^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH51'''<br /> |-<br /> |'''Clan''' <br /> |GH-A<br /> |-<br /> |'''Mechanism'''<br /> |retaining<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |http://www.cazy.org/fam/GH51.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> The majority of the enzymes from this family hydrolyze the glycosidic bond between L-arabinofuranosides side chains of hemicelluloses such as arabinoxylan, arabinogalactan, and L-arabinan. A few enzymes of the family exhibit beta 1-4 endoglucanase activity towards carboxy methyl cellulose and xylan <cite>Eckert2003</cite>. <br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>3</cite>. References that are not in PubMed can be typed in by hand <cite>MikesClassic</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Family GH51 L-arabinfuranosidases are retaining enzymes and follow a classical Koshland double-displacement mechanism. Due to the fast mutarotation and tautomerization rates of arabinose, the stereochemical course of the reaction was determined in presence of methanol and followed by NMR spectroscopy <cite>Pitson1996 Debeche2002 Shallom2002a</cite>. Enzymes that have been well studied kinetically include the ''Geobacillus stearothermophilus'' T-6 and ''Thermobacillus xylanilyticus'' alpha L-arabinofuranosidases, for which a detailed kinetic study was performed including kinetics with aryl-α-L-arabinofuranosides bearing various leaving groups, Brønsted plots for the E175A acid-base catalytic residue and azide-rescue for the E294A nucleophilc mutant <cite>Shallom2002b Debeche2002 Shallom2002a</cite>.<br /> <br /> <br /> == Catalytic Residues ==<br /> Content is to be added here.<br /> <br /> <br /> == Three-dimensional structures ==<br /> Content is to be added here.<br /> <br /> <br /> == Family Firsts ==<br /> ;First sterochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>MikesClassic</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>3</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Eckert2003 pmid=12919323<br /> #Pitson1996 pmid=8946944<br /> #Debeche2002 pmid=11842234<br /> #Shallom2002a pmid=11943144<br /> #Shallom2002b pmid=12221104 <br /> #Comfort2007 pmid=17323919<br /> #He1999 pmid=9312086<br /> #3 isbn=978-0-240-52118-3<br /> #MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH051]]</div>

Yuval Shoham https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_51&diff=4649 Glycoside Hydrolase Family 51 2010-05-10T12:41:34Z

<p>Yuval Shoham: </p> <hr /> <div><br /> {{UnderConstruction}}<br /> * [[Author]]: ^^^Yuval Shoham^^^<br /> * [[Responsible Curator]]: ^^^Yuval Shoham^^^<br /> ----<br /> <br /> <br /> <div style="float:right"><br /> {| {{Prettytable}} <br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH51'''<br /> |-<br /> |'''Clan''' <br /> |GH-A<br /> |-<br /> |'''Mechanism'''<br /> |retaining<br /> |-<br /> |'''Active site residues'''<br /> |known<br /> |-<br /> |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br /> |-<br /> | colspan="2" |http://www.cazy.org/fam/GH51.html<br /> |}<br /> </div><br /> <br /> <br /> <br /> == Substrate specificities ==<br /> Content is to be added here.<br /> <br /> This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below). Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>. You can even cite books using just the ISBN <cite>3</cite>. References that are not in PubMed can be typed in by hand <cite>MikesClassic</cite>. <br /> <br /> <br /> == Kinetics and Mechanism ==<br /> Content is to be added here.<br /> <br /> <br /> == Catalytic Residues ==<br /> Content is to be added here.<br /> <br /> <br /> == Three-dimensional structures ==<br /> Content is to be added here.<br /> <br /> <br /> == Family Firsts ==<br /> ;First sterochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</cite>.<br /> ;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>MikesClassic</cite>.<br /> ;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.<br /> ;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>3</cite>.<br /> <br /> == References ==<br /> <biblio><br /> #Comfort2007 pmid=17323919<br /> #He1999 pmid=9312086<br /> #3 isbn=978-0-240-52118-3<br /> #MikesClassic Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]<br /> <br /> </biblio><br /> <br /> [[Category:Glycoside Hydrolase Families|GH051]]</div>

Yuval Shoham https://www.cazypedia.org/index.php?title=User:Yuval_Shoham&diff=4644 User:Yuval Shoham 2010-05-08T11:42:30Z

<p>Yuval Shoham: Created page with ' Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 …'</p> <hr /> <div> Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 Yuval Shoham is a Professor of Biotechnology at the Technion-Israel Institute of Technology. He obtained his B.Sc. and M.Sc. in Biology and Microbiology from Tel Aviv University and his PhD in Biochemical Engineering from M.I.T under the supervision of Arnold Demain. In 1988 he joined the Technion and his research focuses on: a) the catalytic mechanisms and structure-function relationships of industrial enzymes especially glycoside hydrolases, and b) gene regulation of the hemicellulolytic and cellulolytic systems in Geobacillus stearothermophilus and Clostridium thermocellum.</div>

Yuval Shoham