Glycoside Hydrolase Family 26 - Revision history

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

2021-12-18T21:17:16Z

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

Harry Gilbert: /* Three-dimensional structures */

2018-02-19T20:07:24Z

Three-dimensional structures

Harry Gilbert: /* Family Firsts */

2018-02-19T20:06:28Z

Family Firsts

Harry Gilbert: /* Three-dimensional structures */

2018-02-19T20:06:11Z

Three-dimensional structures

Harry Gilbert: /* References */

2018-02-19T20:05:37Z

References

Harry Gilbert: /* References */

2018-02-19T20:05:07Z

References

Harry Gilbert: /* Three-dimensional structures */

2018-02-19T20:03:25Z

Three-dimensional structures

Harry Gilbert: /* Three-dimensional structures */

2018-02-19T20:02:30Z

Three-dimensional structures

Harry Gilbert: /* References */

2018-02-19T20:02:07Z

References

Harry Gilbert: /* References */

2018-02-19T20:01:42Z

References

@@ Line 1: / Line 1: @@
 {{CuratorApproved}}
-* [[Author]]: ^^^Harry Gilbert^^^
+* [[Author]]: [[User:Harry Gilbert|Harry Gilbert]]
-* [[Responsible Curator]]:  ^^^Henrik Stalbrand^^^
+* [[Responsible Curator]]:  [[User:Henrik Stalbrand|Henrik Stalbrand]]
 ----

@@ Line 34: / Line 34: @@
 == Three-dimensional structures ==
-Three-dimensional structures are available for a large number of Family GH26 enzymes, the first solved being that of the ''Cellvibrio japonicus'' (previously called various names in the genus ''Pseudomonas'') mannanase CjMan26A <cite>Hogg2001</cite>. As members of Clan GHA they have a classical (α/β)<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). The crystal structure of two ''C. japonicus'' mannanases in complex with activated substrates with the acid base mutant <cite>Ducros2002</cite>, or substrates that are very slowly hydrolyzed in the wild type enzyme <cite>Cartmell2008</cite>, show that catalysis by this class of enzyme proceeds via a Boat<sub>2,5</sub> (''B''<sub>2,5</sub>) [[transition state]], whereas the GH26 &beta;-1,3:1,4-glucanase [[transition state]] adopts a half-chair <sup>4</sup>H<sub>3</sub> conformation <cite>Money2008</cite>. The chemical rationale for the different [[transition state]]s adopted by &beta;-mannanases and glucanases is discussed by Davies and colleagues in these publications and elsewhere <cite>Tailford2008</cite>. The crystal structures have also revealed the mechanism of substrate recognition in subsites distal to -1 <cite>LeNours2005,Tailford2009</cite>.
+Three-dimensional structures are available for a large number of Family GH26 enzymes, the first solved being that of the ''Cellvibrio japonicus'' (previously called various names in the genus ''Pseudomonas'') mannanase CjMan26A <cite>Hogg2001</cite>. As members of Clan GHA they have a classical (α/β)<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). The crystal structure of two ''C. japonicus'' mannanases in complex with activated substrates with the acid base mutant <cite>Ducros2002</cite>, or substrates that are very slowly hydrolyzed in the wild type enzyme <cite>Cartmell2008</cite>, show that catalysis by this class of enzyme proceeds via a Boat<sub>2,5</sub> (''B''<sub>2,5</sub>) [[transition state]], whereas the GH26 &beta;-1,3:1,4-glucanase [[transition state]] adopts a half-chair <sup>4</sup>H<sub>3</sub> conformation <cite>Money2006</cite>. The chemical rationale for the different [[transition state]]s adopted by &beta;-mannanases and glucanases is discussed by Davies and colleagues in these publications and elsewhere <cite>Tailford2008</cite>. The crystal structures have also revealed the mechanism of substrate recognition in subsites distal to -1 <cite>LeNours2005,Tailford2009</cite>.
 == Family Firsts ==

@@ Line 40: / Line 40: @@
 ;First [[catalytic nucleophile]] identification: ''Cellvibrio japonicus'' CjMan26A initially by mutagenesis and sequence conservation <cite>Bolam1996</cite> and later by X-ray crystallography <cite>Ducros2002</cite>.
 ;First [[general acid/base]] residue identification: ''Cellvibrio japonicus'' CjMan26A initially be mutagenesis, sequence conservation and kinetics mutant against activated substrate <cite>Bolam1996</cite>.
-;First 3-D structure: ''Cellvibrio japonicus'' CjMan26A <cite>Hogg2000</cite>.
+;First 3-D structure: ''Cellvibrio japonicus'' CjMan26A <cite>Hogg2001</cite>.
 == References ==

@@ Line 34: / Line 34: @@
 == Three-dimensional structures ==
-Three-dimensional structures are available for a large number of Family GH26 enzymes, the first solved being that of the ''Cellvibrio japonicus'' (previously called various names in the genus ''Pseudomonas'') mannanase CjMan26A <cite>Hogg2000</cite>. As members of Clan GHA they have a classical (α/β)<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). The crystal structure of two ''C. japonicus'' mannanases in complex with activated substrates with the acid base mutant <cite>Ducros2002</cite>, or substrates that are very slowly hydrolyzed in the wild type enzyme <cite>Cartmell2008</cite>, show that catalysis by this class of enzyme proceeds via a Boat<sub>2,5</sub> (''B''<sub>2,5</sub>) [[transition state]], whereas the GH26 &beta;-1,3:1,4-glucanase [[transition state]] adopts a half-chair <sup>4</sup>H<sub>3</sub> conformation <cite>Money2008</cite>. The chemical rationale for the different [[transition state]]s adopted by &beta;-mannanases and glucanases is discussed by Davies and colleagues in these publications and elsewhere <cite>Tailford2008</cite>. The crystal structures have also revealed the mechanism of substrate recognition in subsites distal to -1 <cite>LeNours2005,Tailford2009</cite>.
+Three-dimensional structures are available for a large number of Family GH26 enzymes, the first solved being that of the ''Cellvibrio japonicus'' (previously called various names in the genus ''Pseudomonas'') mannanase CjMan26A <cite>Hogg2001</cite>. As members of Clan GHA they have a classical (α/β)<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). The crystal structure of two ''C. japonicus'' mannanases in complex with activated substrates with the acid base mutant <cite>Ducros2002</cite>, or substrates that are very slowly hydrolyzed in the wild type enzyme <cite>Cartmell2008</cite>, show that catalysis by this class of enzyme proceeds via a Boat<sub>2,5</sub> (''B''<sub>2,5</sub>) [[transition state]], whereas the GH26 &beta;-1,3:1,4-glucanase [[transition state]] adopts a half-chair <sup>4</sup>H<sub>3</sub> conformation <cite>Money2008</cite>. The chemical rationale for the different [[transition state]]s adopted by &beta;-mannanases and glucanases is discussed by Davies and colleagues in these publications and elsewhere <cite>Tailford2008</cite>. The crystal structures have also revealed the mechanism of substrate recognition in subsites distal to -1 <cite>LeNours2005,Tailford2009</cite>.
 == Family Firsts ==

@@ Line 49: / Line 49: @@
 #Bolam1996 pmid=8973192
 #Ducros2002 pmid=12203498
-#Hogg2000 pmid=11382747
+#Hogg2001 pmid=11382747
 #Money2006 pmid=16823793
 #Tailford2008 pmid=18408714

@@ Line 53: / Line 53: @@
 #Tailford2008 pmid=18408714
 #LeNours2005 pmid=16171384
-#1Tailford2009 pmid=19441796
+#Tailford2009 pmid=19441796
 #Gilkes1991 pmid=1886523
 </biblio>
 [[Category:Glycoside Hydrolase Families|GH026]]

@@ Line 45: / Line 45: @@
 <biblio>
 #Cartmell2008 pmid=18799462
-#2 pmid=15987675
+#Taylor2005 pmid=15987675
-#3 pmid=10742274
+#Araki2000 pmid=10742274
-#4 pmid=8973192
+#Bolam1996 pmid=8973192
-#5 pmid=12203498
+#Ducros2002 pmid=12203498
-#6 pmid=11382747
+#Hogg2000 pmid=11382747
-#7 pmid=16823793
+#Money2006 pmid=16823793
-#8 pmid=18408714
+#Tailford2008 pmid=18408714
-#9 pmid=16171384
+#Le Nours2005 pmid=16171384
-#10 pmid=19441796
+#1Tailford2009 pmid=19441796
 #Gilkes1991 pmid=1886523
 </biblio>
 [[Category:Glycoside Hydrolase Families|GH026]]