Glycoside Hydrolase Family 10 - Revision history

Harry Brumer: /* Kinetics and Mechanism */

2015-07-29T16:43:45Z

Kinetics and Mechanism

Harry Brumer at 16:41, 29 July 2015

2015-07-29T16:41:45Z

Harry Brumer at 16:20, 29 July 2015

2015-07-29T16:20:28Z

Harry Brumer: updated CAZyDBlink

2012-09-10T16:32:04Z

updated CAZyDBlink

Spencer Williams at 11:45, 14 June 2010

2010-06-14T11:45:59Z

Harry Brumer at 13:54, 8 November 2009

2009-11-08T13:54:36Z

Spencer Williams at 02:08, 1 September 2009

2009-09-01T02:08:29Z

Spencer Williams at 12:19, 25 August 2009

2009-08-25T12:19:42Z

Harry Brumer at 19:20, 30 July 2009

2009-07-30T19:20:10Z

Harry Brumer at 21:51, 19 June 2009

2009-06-19T21:51:24Z

@@ Line 33: / Line 33: @@
 ____________
-<nowiki>*</nowiki> This enzyme has frequently (and erroneously) been called [[exo]]-cellulase in the literature (hence the name Cex). The error came from the low, but significant activity of the enzyme on aryl-beta-cellobioside, a substrate once thought to be specific of [[exo]]-cellulases. Although everyone agrees now that this is an [[endo]]-1,4-xylanase, the Vancouver group still calls it Cex "[[endo]]-glycanase" instead of calling it xylanase CfXyn10A <cite>10</cite>. Prior to extensive biochemical analysis, GH10 was one of the first glycoside hydrolase families classified by hydrophobic cluster analysis, and was previously known as "Cellulase Family F" <cite>Henrissat1989 Gilkes1991</cite>.
+<nowiki>*</nowiki> This enzyme has frequently (and erroneously) been called [[exo]]-cellulase in the literature (hence the name Cex). The error came from the low, but significant activity of the enzyme on aryl-beta-cellobioside, a substrate once thought to be specific of [[exo]]-cellulases. Although everyone agrees now that this is an [[endo]]-1,4-xylanase, the Vancouver group still calls it Cex "[[endo]]-glycanase" instead of calling it xylanase CfXyn10A <cite>10</cite>. Indeed, prior to extensive biochemical analysis, GH10 was one of the first glycoside hydrolase families classified by hydrophobic cluster analysis, and was previously known as "Cellulase Family F" <cite>Henrissat1989 Gilkes1991</cite>.
 == Catalytic Residues ==

@@ Line 33: / Line 33: @@
 ____________
-<nowiki>*</nowiki> This enzyme has frequently (and erroneously) been called [[exo]]-cellulase in the literature (hence the name Cex). The error came from the low, but significant activity of the enzyme on aryl-beta-cellobioside, a substrate once thought to be specific of [[exo]]-cellulases. Although everyone agrees now that this is an [[endo]]-1,4-xylanase, the Vancouver group still calls it Cex "[[endo]]-glycanase" instead of calling it xylanase CfXyn10A <cite>10</cite>. Prior to detailed biochemical analysis, GH10 was one of the first glycoside hydrolase families classified by hydrophobic cluster analysis, and was previously known as "Cellulase Family F" <cite>Henrissat1989 Gilkes1991</cite>.
+<nowiki>*</nowiki> This enzyme has frequently (and erroneously) been called [[exo]]-cellulase in the literature (hence the name Cex). The error came from the low, but significant activity of the enzyme on aryl-beta-cellobioside, a substrate once thought to be specific of [[exo]]-cellulases. Although everyone agrees now that this is an [[endo]]-1,4-xylanase, the Vancouver group still calls it Cex "[[endo]]-glycanase" instead of calling it xylanase CfXyn10A <cite>10</cite>. Prior to extensive biochemical analysis, GH10 was one of the first glycoside hydrolase families classified by hydrophobic cluster analysis, and was previously known as "Cellulase Family F" <cite>Henrissat1989 Gilkes1991</cite>.
 == Catalytic Residues ==

@@ Line 33: / Line 33: @@
 ____________
-<nowiki>*</nowiki> This enzyme has frequently (and erroneously) been called [[exo]]-cellulase in the literature (hence the name Cex). The error came from the low, but significant activity of the enzyme on aryl-beta-cellobioside, a substrate once thought to be specific of [[exo]]-cellulases. Although everyone agrees now that this is an [[endo]]-1,4-xylanase, the Vancouver group still calls it Cex "[[endo]]-glycanase" instead of calling it xylanase CfXyn10A <cite>10</cite>.
+<nowiki>*</nowiki> This enzyme has frequently (and erroneously) been called [[exo]]-cellulase in the literature (hence the name Cex). The error came from the low, but significant activity of the enzyme on aryl-beta-cellobioside, a substrate once thought to be specific of [[exo]]-cellulases. Although everyone agrees now that this is an [[endo]]-1,4-xylanase, the Vancouver group still calls it Cex "[[endo]]-glycanase" instead of calling it xylanase CfXyn10A <cite>10</cite>. Prior to detailed biochemical analysis, GH10 was one of the first glycoside hydrolase families classified by hydrophobic cluster analysis, and was previously known as "Cellulase Family F" <cite>Henrissat1989 Gilkes1991</cite>.
 == Catalytic Residues ==
@@ Line 40: / Line 40: @@
 == Three-dimensional structures ==
 Three-dimensional structures are available for a large number of Family GH10 enzymes, the first solved being those of the ''Streptomyces lividans'' xylanase A <cite>7</cite>, the ''C. fimi'' endo-glycanase Cex <cite>8</cite>, and the ''Cellvibrio japonicus'' Xyn10A (previously ''Pseudomonas fluorescens'' subsp. xylanase A)  <cite>HJG</cite>. As members of Clan GHA they have a classical (&alpha;/&beta;)<sub>8</sub> TIM barrel fold with the two key active site glutamic acids located at the C-terminal ends of beta-strands 4 (acid/base) and 7 (nucleophile) <cite>9</cite>.
 == Family Firsts ==
@@ Line 61: / Line 60: @@
 #10 pmid=9559678
 #HJG pmid=7881909
 </biblio>
 [[Category:Glycoside Hydrolase Families|GH010]]

@@ Line 21: / Line 21: @@
 |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 |-
-| colspan="2" |http://www.cazy.org/fam/GH10.html
+| colspan="2" |{{CAZyDBlink}}GH10.html
 |}
 </div>

@@ Line 36: / Line 36: @@
 == Catalytic Residues ==
-The [[catalytic nucleophile]] was first identified in the ''Cellulomonas fimi'' [[endo]]-xylanase (CfXyn10A) as Glu233 (earlier numbered as 274) in the sequence IT'''<u>E</u>'''LD through trapping of the 2-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and subsequent peptide mapping <cite>5</cite>. The [[general acid/base]] catalyst was first identified as Glu127 in this same enzyme through detailed mechanistic analysis of mutants at that position, which included azide rescue experiments <cite>6</cite>. Family GH10 enzymes, as is typical of [http://www.cazy.org/fam/acc_GH.html#table Clan GHA], have an asparagine residue preceding the acid/base catalyst in a typical NEP sequence. The asparagine engages in important hydrogen bonding interactions with the substrate 2-hydroxyl.
+The [[catalytic nucleophile]] was first identified in the ''Cellulomonas fimi'' [[endo]]-xylanase (CfXyn10A) as Glu233 (earlier numbered as 274) in the sequence IT'''<u>E</u>'''LD through trapping of the 2-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and subsequent peptide mapping <cite>5</cite>. The [[general acid/base]] residue was first identified as Glu127 in this same enzyme through detailed mechanistic analysis of mutants at that position, which included azide rescue experiments <cite>6</cite>. Family GH10 enzymes, as is typical of [http://www.cazy.org/fam/acc_GH.html#table Clan GHA], have an asparagine residue preceding the [[general acid/base]] residue in a typical NEP sequence. The asparagine engages in important hydrogen-bonding interactions with the substrate 2-hydroxyl.
 == Three-dimensional structures ==

← Older revision		Revision as of 13:54, 8 November 2009
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		+	{{CuratorApproved}}
	* [[Author]]: [[User:Withers\|Stephen Withers]]		* [[Author]]: [[User:Withers\|Stephen Withers]]
	* [[Responsible Curator]]: [[User:Withers\|Stephen Withers]]		* [[Responsible Curator]]: [[User:Withers\|Stephen Withers]]

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 == Substrate specificities ==
-Although a few members of this family show [[endo]]-beta-1,3-xylanase activity, the majority of the enzymes are [[endo]]-beta-1,4-xylanases. Some of the latter display limited activity on aryl cellobiosides, but not on cellulose.
+Although a few [[glycoside hydrolases]] of this family show [[endo]]-beta-1,3-xylanase activity, the majority of the enzymes are [[endo]]-beta-1,4-xylanases. Some of the latter display limited activity on aryl cellobiosides, but not on cellulose.
 == Kinetics and Mechanism ==
@@ Line 35: / Line 35: @@
 == Catalytic Residues ==
-The catalytic nucleophile was first identified in the ''Cellulomonas fimi'' [[endo]]-xylanase (CfXyn10A) as Glu233 (earlier numbered as 274) in the sequence IT'''<u>E</u>'''LD through trapping of the 2-deoxy-2-fluoroglucosyl-enzyme intermediate and subsequent peptide mapping <cite>5</cite>. The acid/base catalyst was first identified as Glu127 in this same enzyme through detailed mechanistic analysis of mutants at that position, which included azide rescue experiments <cite>6</cite>. Family GH10 enzymes, as is typical of [http://www.cazy.org/fam/acc_GH.html#table Clan GHA], have an asparagine residue preceding the acid/base catalyst in a typical NEP sequence. The asparagine engages in important hydrogen bonding interactions with the substrate 2-hydroxyl.
+The [[catalytic nucleophile]] was first identified in the ''Cellulomonas fimi'' [[endo]]-xylanase (CfXyn10A) as Glu233 (earlier numbered as 274) in the sequence IT'''<u>E</u>'''LD through trapping of the 2-deoxy-2-fluoroglucosyl-enzyme [[intermediate]] and subsequent peptide mapping <cite>5</cite>. The [[general acid/base]] catalyst was first identified as Glu127 in this same enzyme through detailed mechanistic analysis of mutants at that position, which included azide rescue experiments <cite>6</cite>. Family GH10 enzymes, as is typical of [http://www.cazy.org/fam/acc_GH.html#table Clan GHA], have an asparagine residue preceding the acid/base catalyst in a typical NEP sequence. The asparagine engages in important hydrogen bonding interactions with the substrate 2-hydroxyl.
 == Three-dimensional structures ==
@@ Line 43: / Line 43: @@
 == Family Firsts ==
 ;First sterochemistry determination: ''Cellulomonas fimi'' endo-xylanase Cex (CfXyn10A) by NMR <cite>1</cite>
-;First catalytic nucleophile identification: ''Cellulomonas fimi'' endo-xylanase Cex (CfXyn10A) by 2-fluoroglucose labeling <cite>5</cite>
+;First [[catalytic nucleophile]] identification: ''Cellulomonas fimi'' endo-xylanase Cex (CfXyn10A) by 2-fluoroglucose labeling <cite>5</cite>
-;First general acid/base residue identification: ''Cellulomonas fimi'' endo-xylanase Cex (CfXyn10A) by rescue kinetics with mutants <cite>6</cite>
+;First [[general acid/base]] residue identification: ''Cellulomonas fimi'' endo-xylanase Cex (CfXyn10A) by rescue kinetics with mutants <cite>6</cite>
 ;First 3-dimensional structure: ''Cellulomonas fimi'' endo-xylanase Cex (CfXyn10A) <cite>8</cite>,  ''Streptomyces lividans'' xylanase (SlXyn10A) <cite>7</cite>, and ''Cellvibrio japonicus'' Xyn10A (previously ''Pseudomonas fluorescens'' subsp. xylanase A) <cite>HJG</cite>.

← Older revision		Revision as of 19:20, 30 July 2009
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	</biblio>		</biblio>

−	[[Category:Glycoside Hydrolase Families]]	+	[[Category:Glycoside Hydrolase Families\|GH010]]

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-* Author: [[User:Withers|Stephen Withers]]
+* [[Author]]: [[User:Withers|Stephen Withers]]
-* Responsible Editor:  [[User:Withers|Stephen Withers]]
+* [[Responsible Curator]]:  [[User:Withers|Stephen Withers]]
 ----