Glycoside Hydrolase Family 80 - Revision history

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

2021-12-18T21:15:44Z

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

Spencer Williams at 11:25, 24 July 2011

2011-07-24T11:25:45Z

Harry Brumer at 13:37, 18 July 2011

2011-07-18T13:37:17Z

Harry Brumer: /* Three-dimensional structures */

2011-07-18T13:11:17Z

Three-dimensional structures

Harry Brumer at 13:05, 18 July 2011

2011-07-18T13:05:45Z

Harry Brumer at 13:00, 18 July 2011

2011-07-18T13:00:19Z

Ryszard Brzezinski at 16:38, 15 July 2011

2011-07-15T16:38:35Z

Ryszard Brzezinski at 16:37, 15 July 2011

2011-07-15T16:37:53Z

Ryszard Brzezinski at 16:56, 14 July 2011

2011-07-14T16:56:35Z

Ryszard Brzezinski at 16:52, 14 July 2011

2011-07-14T16:52:52Z

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 <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
 {{CuratorApproved}}
-* [[Author]]: ^^^Ryszard Brzezinski^^^
+* [[Author]]: [[User:Ryszard Brzezinski|Ryszard Brzezinski]]
-* [[Responsible Curator]]:  ^^^Ryszard Brzezinski^^^
+* [[Responsible Curator]]:  [[User:Ryszard Brzezinski|Ryszard Brzezinski]]
 ----

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 == Substrate specificities ==
-Glycoside hydrolase family GH80 is comprised of endo-acting beta-1,4-chitosanases of bacterial origin. The first characterized member was from a proteobacterium <cite>Park1999</cite> belonging to the Bacteroidetes/Chlorobi group <cite>Matsuda2001 Yi2004</cite>.  At present (July 2011), GH80 is very small family, comprised of fewer than 20 members.
+[[Glycoside hydrolase]] family GH80 is comprised of ''[[endo]]''-acting &beta;-1,4-chitosanases of bacterial origin. The first characterized member was from a proteobacterium <cite>Park1999</cite> belonging to the Bacteroidetes/Chlorobi group <cite>Matsuda2001 Yi2004</cite>.  At present (July 2011), GH80 is very small family, comprised of fewer than 20 members.
 Characterized GH80 members do not hydrolyze chitin or cellulose <cite>Park1999 Yi2004</cite>, and for one member, the chitosan hexa-oligosaccharide (GlcN)<sub>6</sub> is preferentially hydrolyzed into two molecules of the trisaccharide <cite>Shimono2002</cite>.
@@ Line 37: / Line 37: @@
 == Catalytic Residues ==
-The chitosanases from family GH80 share a PROSITE signature motif <cite>Sigrist2010</cite> with the chitosanases from family [[GH46]] <cite>Tremblay2000</cite>.  Together with [[GH24]], these three families comprise [[Clan]] GH-I <cite>CAZYGHpage</cite>.
+The chitosanases from family GH80 share a PROSITE signature motif <cite>Sigrist2010</cite> with the chitosanases from family [[GH46]] <cite>Tremblay2000</cite>.  Together with [[GH24]], these three families comprise [[clan]] GH-I <cite>CAZYGHpage</cite>.
 A site-directed mutagenesis study of the chitosanase A from ''Matsuebacter chitosanotabidus'' 3001 (new name: ''Mitsuaria chitosanitabida'' <cite>Amakata2005</cite>) identified two residues as essentiel for catalysis: Glu-121 (in the sequence YP<u>E</u>NG)and Glu-141 (in the sequence DY<u>E</u>AA) <cite>Shimono2002</cite>.
 == Three-dimensional structures ==
-No three-dimensional structure has yet been solved for this family.  As a member of [[Clan]] GH-I, a lysozyme-like &alpha;-&beta; fold is suggested, based on known [[GH24]] and [[GH46]] structures.
+No three-dimensional structure has yet been solved for this family.  As a member of [[clan]] GH-I, a lysozyme-like &alpha;-&beta; fold is suggested, based on known [[GH24]] and [[GH46]] structures.
 == Family Firsts ==

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 #Amakata2005 pmid=16166689
 #CAZYGHpage http://www.cazy.org/Glycoside-Hydrolases.html
 [[Category:Glycoside Hydrolase Families|GH080]]

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 == Three-dimensional structures ==
-No three-dimensional structure has yet been solved for this family.
+No three-dimensional structure has yet been solved for this family.  As a member of [[Clan]] GH-I, a lysozyme-like &alpha;-&beta; fold is suggested, based on known [[GH24]] and [[GH46]] structures.
 == Family Firsts ==

@@ Line 34: / Line 34: @@
 == Kinetics and Mechanism ==
-The stereochemistry of the hydrolytic reaction catalyzed by GH80 members has not yet been studied. However, sequence similarity with members of [[Clan]] GH-I suggests that these enzymes may operate with inversion of the anomeric configuration (see [[#Catalytic Residues]], below)
+The stereochemistry of the hydrolytic reaction catalyzed by GH80 members has not yet been studied. However, sequence similarity with members of [[Clan]] GH-I suggests that these enzymes may operate with inversion of the anomeric configuration (see ''Catalytic Residues'', below)
 == Catalytic Residues ==
-The chitosanases from family GH80 share a PROSITE signature motif with the chitosanases from family GH46 <cite>Tremblay2000 Sigrist2010</cite>.
+The chitosanases from family GH80 share a PROSITE signature motif <cite>Sigrist2010</cite> with the chitosanases from family [[GH46]] <cite>Tremblay2000</cite>.  Together with [[GH24]], these three families comprise [[Clan]] GH-I <cite>CAZYGHpage</cite>.
 A site-directed mutagenesis study of the chitosanase A from ''Matsuebacter chitosanotabidus'' 3001 (new name: ''Mitsuaria chitosanitabida'' <cite>Amakata2005</cite>) identified two residues as essentiel for catalysis: Glu-121 (in the sequence YP<u>E</u>NG)and Glu-141 (in the sequence DY<u>E</u>AA) <cite>Shimono2002</cite>.
 == Three-dimensional structures ==
-No three-dimensional structure has been solved for this family.
+No three-dimensional structure has yet been solved for this family.
 == Family Firsts ==
@@ Line 61: / Line 60: @@
 #Sigrist2010 pmid=19858104
 #Amakata2005 pmid=16166689
+#CAZYGHpage http://www.cazy.org/Glycoside-Hydrolases.html
 [[Category:Glycoside Hydrolase Families|GH080]]

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 == Catalytic Residues ==
-A site-directed mutagenesis study of the chitosanase A from Matsuebacter chitosanotabidus 3001 (new name: Mitsuaria chitosanitabida <cite>Amakata2005</cite>) identified two residues as essentiel for catalysis: Glu-121 (in the sequence YP<u>E</u>NG)and Glu-141 (in the sequence DY<u>E</u>AA) <cite>Shimono2002</cite>.
+A site-directed mutagenesis study of the chitosanase A from ''Matsuebacter chitosanotabidus'' 3001 (new name: ''Mitsuaria chitosanitabida'' <cite>Amakata2005</cite>) identified two residues as essentiel for catalysis: Glu-121 (in the sequence YP<u>E</u>NG)and Glu-141 (in the sequence DY<u>E</u>AA) <cite>Shimono2002</cite>.
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 == Family Firsts ==
-;First primary sequence determination: Chitosanase ChoA from Matsuebacter chitosanotabidus 3001 (now Mitsuaria chitosanitabida) <cite>Park1999 Amakata2005</cite>
+;First primary sequence determination: Chitosanase ChoA from ''Matsuebacter chitosanotabidus'' 3001 (now ''Mitsuaria chitosanitabida'') <cite>Park1999 Amakata2005</cite>
 ;First stereochemistry determination: Not yet determined
 ;First catalytic nucleophile identification: Not yet identified
@@ Line 56: / Line 56: @@
 <biblio>
 #Park1999 pmid=10542164
-#Matsuda2001 Matsuda, Y., Iida, I., Shinogi, T., Kakutani, K., Nonomura, T., Toyoda, H. (2001) ''In vitro'' suppression of mycelial growth of ''Fusarium oxysporum'' by extracellular chitosanase of ''Sphingobacterium multivorum'' and cloning of the chitosanase gene ''csn''SM1. J. Gen. Plant Pathol. 67, 318-324.
+#Matsuda2001 Matsuda, Y., Iida, I., Shinogi, T., Kakutani, K., Nonomura, T., Toyoda, H. (2001) ''In vitro suppression of mycelial growth of Fusarium oxysporum by extracellular chitosanase of Sphingobacterium multivorum and cloning of the chitosanase gene csnSM1.'' J. Gen. Plant Pathol. 67, 318-324.
-#Yi2004 Yi, J.-H., Jang, H.-K., Lee, S.-J., Lee, K.-E., Choi, S.-G. (2004) Purification and properties of chitosanase from chitinolytic beta-Proteobacterium KNU3. J. Microbiol. Biotechnol. 14, 337-343.
+#Yi2004 Yi, J.-H., Jang, H.-K., Lee, S.-J., Lee, K.-E., Choi, S.-G. (2004) ''Purification and properties of chitosanase from chitinolytic beta-Proteobacterium KNU3''. J. Microbiol. Biotechnol. 14, 337-343.
 #Shimono2002 pmid=11754739
 #Tremblay2000 pmid=11068683

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 == Substrate specificities ==
 Glycoside hydrolases of family 80 include bacterial proteins. They were characterized from proteobacteria <cite>Park1999</cite> of from species belonging to the Bacteroidetes/Chlorobi group <cite>Matsuda2001 Yi2004</cite>. They are beta-1,4-chitosanases with endo-splitting activity. Chitin or cellulose are not hydrolyzed <cite>Park1999 Yi2004</cite>. Chitosan hexamer (GlcN)<sub>6</sub> is preferentially hydrolyzed into two trimeric molecules <cite>Shimono2002</cite>.
-new sentence here<cite>Tremblay2000 Sigrist2010</cite>
+The chitosanases from family GH80 share a PROSITE signature motif with the chitosanases from family GH46 <cite>Tremblay2000 Sigrist2010</cite>.
 == Kinetics and Mechanism ==
-Content is to be added here.
+No detailed studies available yet.
 == Catalytic Residues ==
-Content is to be added here.
+A site-directed mutagenesis study of the chitosanase A from Matsuebacter chitosanotabidus 3001 (new name: Mitsuaria chitosanitabida <cite>Amakata2005</cite>) identified two residues as essentiel for catalysis: Glu-121 (in the sequence YP<u>E</u>NG)and Glu-141 (in the sequence DY<u>E</u>AA) <cite>Shimono2002</cite>.
 == Three-dimensional structures ==
-Content is to be added here.
+No three-dimensional structure has been solved for this family.
 == Family Firsts ==
 ;First primary sequence determination: Chitosanase ChoA from Matsuebacter chitosanotabidus 3001 (now Mitsuaria chitosanitabida) <cite>Park1999 Amakata2005</cite>
-;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation .
+;First stereochemistry determination: Not yet determined
-;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation .
+;First catalytic nucleophile identification: Not yet identified
-;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation .
+;First general acid/base residue identification: Not yet identified
-;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation.
+;First 3-D structure: Not yet determined
 == References ==