Glycoside Hydrolase Family 51 - Revision history

Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

2021-12-18T21:18:45Z

Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

Harry Brumer: removed old biblio references

2013-06-04T15:32:41Z

removed old biblio references

Harry Brumer: updated CAZyDBlink

2012-09-10T16:38:53Z

updated CAZyDBlink

Spencer Williams: /* Catalytic Residues */

2010-06-09T11:42:15Z

Catalytic Residues

Spencer Williams: /* Catalytic Residues */

2010-06-09T11:41:58Z

Catalytic Residues

Spencer Williams at 11:41, 9 June 2010

2010-06-09T11:41:42Z

Yuval Shoham at 15:21, 12 May 2010

2010-05-12T15:21:29Z

Yuval Shoham at 15:19, 12 May 2010

2010-05-12T15:19:52Z

Yuval Shoham: /* Kinetics and Mechanism */

2010-05-10T17:37:57Z

Kinetics and Mechanism

Yuval Shoham: /* Family Firsts */

2010-05-10T17:35:53Z

Family Firsts

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-* [[Author]]: ^^^Yuval Shoham^^^
+* [[Author]]: [[User:Yuval Shoham|Yuval Shoham]]
-* [[Responsible Curator]]:  ^^^Yuval Shoham^^^
+* [[Responsible Curator]]:  [[User:Yuval Shoham|Yuval Shoham]]
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 #Paes2008 pmid=18563919
 </biblio>
 [[Category:Glycoside Hydrolase Families|GH051]]

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 |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 |-
-| colspan="2" |http://www.cazy.org/fam/GH51.html
+| colspan="2" |{{CAZyDBlink}}GH51.html
 |}
 </div>

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 == Catalytic Residues ==
-The [[general 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.
+The [[general 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.
 == Three-dimensional structures ==

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 == Catalytic Residues ==
-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.
+The [[general 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.
 == Three-dimensional structures ==

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 == Substrate specificities ==
-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>.
+The majority of the [[glycoside hydrolase]]s 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 carboxymethyl cellulose and xylan <cite>Eckert2003</cite>.
 == Kinetics and Mechanism ==
-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>.
+GH51 L-arabinfuranosidases are [[retaining]] enzymes and follow a [[classical Koshland retaining mechanism]].  Owing to the fast mutarotation and tautomerization rates of arabinose, the stereochemical course of the reaction was monitored 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>.
 == Catalytic Residues ==
-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.
+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.
 == Three-dimensional structures ==
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 == Family Firsts ==
 ;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>.
-;First catalytic nucleophile identification: ''Geobacillus stearothermophilus'' α-L-arabinofuranosidase  through detailed kinetic studies for the catalytic mutant including azide rescue <cite>Shallom2002b</cite>.
+;First [[catalytic nucleophile]] identification: ''Geobacillus stearothermophilus'' α-L-arabinofuranosidase  through detailed kinetic studies for the catalytic mutant including azide rescue <cite>Shallom2002b</cite>.
-;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>.
+;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>.
 ;First 3-D structure: ''Geobacillus stearothermophilus'' α-L-arabinofuranosidase <cite>Hovel2003</cite>.