https://www.cazypedia.org/api.php?action=feedcontributions&feedformat=atom&user=Ryszard+BrzezinskiCAZypedia - User contributions [en-ca]2026-05-05T00:01:47ZUser contributionsMediaWiki 1.35.10https://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_80&diff=6929Glycoside Hydrolase Family 802011-07-15T16:38:35Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH80'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|not determined<br />
|-<br />
|'''Active site residues'''<br />
|inferred<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH80.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
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>.<br />
The chitosanases from family GH80 share a PROSITE signature motif with the chitosanases from family GH46 <cite>Tremblay2000 Sigrist2010</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
No detailed studies available yet.<br />
<br />
<br />
== Catalytic Residues ==<br />
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>.<br />
<br />
<br />
== Three-dimensional structures ==<br />
No three-dimensional structure has been solved for this family.<br />
<br />
<br />
== Family Firsts ==<br />
;First primary sequence determination: Chitosanase ChoA from ''Matsuebacter chitosanotabidus'' 3001 (now ''Mitsuaria chitosanitabida'') <cite>Park1999 Amakata2005</cite><br />
;First stereochemistry determination: Not yet determined<br />
;First catalytic nucleophile identification: Not yet identified<br />
;First general acid/base residue identification: Not yet identified<br />
;First 3-D structure: Not yet determined<br />
<br />
== References ==<br />
<biblio><br />
#Park1999 pmid=10542164<br />
#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.<br />
#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.<br />
#Shimono2002 pmid=11754739<br />
#Tremblay2000 pmid=11068683<br />
#Sigrist2010 pmid=19858104<br />
#Amakata2005 pmid=16166689<br />
<br />
<br />
<br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH080]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_80&diff=6928Glycoside Hydrolase Family 802011-07-15T16:37:53Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH80'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|not determined<br />
|-<br />
|'''Active site residues'''<br />
|inferred<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH80.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
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>.<br />
The chitosanases from family GH80 share a PROSITE signature motif with the chitosanases from family GH46 <cite>Tremblay2000 Sigrist2010</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
No detailed studies available yet.<br />
<br />
<br />
== Catalytic Residues ==<br />
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>.<br />
<br />
<br />
== Three-dimensional structures ==<br />
No three-dimensional structure has been solved for this family.<br />
<br />
<br />
== Family Firsts ==<br />
;First primary sequence determination: Chitosanase ChoA from ''Matsuebacter chitosanotabidus'' 3001 (now ''Mitsuaria chitosanitabida'') <cite>Park1999 Amakata2005</cite><br />
;First stereochemistry determination: Not yet determined<br />
;First catalytic nucleophile identification: Not yet identified<br />
;First general acid/base residue identification: Not yet identified<br />
;First 3-D structure: Not yet determined<br />
<br />
== References ==<br />
<biblio><br />
#Park1999 pmid=10542164<br />
#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.<br />
#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.<br />
#Shimono2002 pmid=11754739<br />
#Tremblay2000 pmid=11068683<br />
#Sigrist2010 pmid=19858104<br />
#Amakata2005 pmid=16166689<br />
<br />
<br />
<br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH080]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_80&diff=6927Glycoside Hydrolase Family 802011-07-14T16:56:35Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH80'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|not determined<br />
|-<br />
|'''Active site residues'''<br />
|inferred<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH80.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
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>.<br />
The chitosanases from family GH80 share a PROSITE signature motif with the chitosanases from family GH46 <cite>Tremblay2000 Sigrist2010</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
No detailed studies available yet.<br />
<br />
<br />
== Catalytic Residues ==<br />
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>.<br />
<br />
<br />
== Three-dimensional structures ==<br />
No three-dimensional structure has been solved for this family.<br />
<br />
<br />
== Family Firsts ==<br />
;First primary sequence determination: Chitosanase ChoA from ''Matsuebacter chitosanotabidus'' 3001 (now ''Mitsuaria chitosanitabida'') <cite>Park1999 Amakata2005</cite><br />
;First stereochemistry determination: Not yet determined<br />
;First catalytic nucleophile identification: Not yet identified<br />
;First general acid/base residue identification: Not yet identified<br />
;First 3-D structure: Not yet determined<br />
<br />
== References ==<br />
<biblio><br />
#Park1999 pmid=10542164<br />
#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.<br />
#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.<br />
#Shimono2002 pmid=11754739<br />
#Tremblay2000 pmid=11068683<br />
#Sigrist2010 pmid=19858104<br />
#Amakata2005 pmid=16166689<br />
<br />
<br />
<br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH080]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_80&diff=6926Glycoside Hydrolase Family 802011-07-14T16:52:52Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH80'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|not determined<br />
|-<br />
|'''Active site residues'''<br />
|inferred<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH80.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
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>.<br />
The chitosanases from family GH80 share a PROSITE signature motif with the chitosanases from family GH46 <cite>Tremblay2000 Sigrist2010</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
No detailed studies available yet.<br />
<br />
<br />
== Catalytic Residues ==<br />
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>.<br />
<br />
<br />
== Three-dimensional structures ==<br />
No three-dimensional structure has been solved for this family.<br />
<br />
<br />
== Family Firsts ==<br />
;First primary sequence determination: Chitosanase ChoA from Matsuebacter chitosanotabidus 3001 (now Mitsuaria chitosanitabida) <cite>Park1999 Amakata2005</cite><br />
;First stereochemistry determination: Not yet determined<br />
;First catalytic nucleophile identification: Not yet identified<br />
;First general acid/base residue identification: Not yet identified<br />
;First 3-D structure: Not yet determined<br />
<br />
== References ==<br />
<biblio><br />
#Park1999 pmid=10542164<br />
#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.<br />
#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.<br />
#Shimono2002 pmid=11754739<br />
#Tremblay2000 pmid=11068683<br />
#Sigrist2010 pmid=19858104<br />
#Amakata2005 pmid=16166689<br />
<br />
<br />
<br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH080]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_80&diff=6925Glycoside Hydrolase Family 802011-07-14T16:41:39Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH80'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|not determined<br />
|-<br />
|'''Active site residues'''<br />
|inferred<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH80.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
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>.<br />
new sentence here<cite>Tremblay2000 Sigrist2010</cite><br />
<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 primary sequence determination: Chitosanase ChoA from Matsuebacter chitosanotabidus 3001 (now Mitsuaria chitosanitabida) <cite>Park1999 Amakata2005</cite><br />
;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation.<br />
<br />
== References ==<br />
<biblio><br />
#Park1999 pmid=10542164<br />
#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.<br />
#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.<br />
#Shimono2002 pmid=11754739<br />
#Tremblay2000 pmid=11068683<br />
#Sigrist2010 pmid=19858104<br />
#Amakata2005 pmid=16166689<br />
<br />
<br />
<br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH080]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_80&diff=6924Glycoside Hydrolase Family 802011-07-12T20:51:02Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH80'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|not determined<br />
|-<br />
|'''Active site residues'''<br />
|inferred<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH80.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
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>.<br />
new sentence here<cite>Shimono2002</cite><br />
new sentence here<cite>Tremblay2000 Sigrist2010</cite><br />
<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 primary sequence determination: Chitosanase ChoA from Matsuebacter chitosanotabidus 3001 (now Mitsuaria chitosanitabida) <cite>Park1999 Amakata2005</cite><br />
;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation.<br />
<br />
== References ==<br />
<biblio><br />
#Park1999 pmid=10542164<br />
#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.<br />
#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.<br />
#Shimono2002 pmid=11754739<br />
#Tremblay2000 pmid=11068683<br />
#Sigrist2010 pmid=19858104<br />
#Amakata2005 pmid=16166689<br />
<br />
<br />
<br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH080]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_80&diff=6923Glycoside Hydrolase Family 802011-07-12T20:48:31Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH80'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|not determined<br />
|-<br />
|'''Active site residues'''<br />
|inferred<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH80.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
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>.<br />
new sentence here<cite>Shimono2002</cite><br />
new sentence here<cite>Tremblay2000 Sigrist2010</cite><br />
<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 primary sequence determination: Chitosanase ChoA from Matsuebacter chitosanotabidus 3001 (now Mitsuaria chitosanitabida) <cite>Park1999 Amakata2005</cite><br />
;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation.<br />
<br />
== References ==<br />
<biblio><br />
#Park1999 pmid=10542164<br />
#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.<br />
#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.<br />
#Shimono2002 pmid=11754739<br />
#Tremblay2000 pmid=11068683<br />
#Sigrist2010 pmid=19858104<br />
<br />
<br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH080]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_80&diff=6922Glycoside Hydrolase Family 802011-07-12T20:47:11Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH80'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|not determined<br />
|-<br />
|'''Active site residues'''<br />
|inferred<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH80.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
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>.<br />
new sentence here<cite>Shimono2002</cite><br />
new sentence here<cite>Tremblay2000 Sigrist2010</cite><br />
<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 primary sequence determination: Chitosanase ChoA from Matsuebacter chitosanotabidus 3001 (now Mitsuaria chitosanitabida) <cite Park1999 Amakata2005</cite><br />
;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation.<br />
<br />
== References ==<br />
<biblio><br />
#Park1999 pmid=10542164<br />
#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.<br />
#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.<br />
#Shimono2002 pmid=11754739<br />
#Tremblay2000 pmid=11068683<br />
#Sigrist2010 pmid=19858104<br />
<br />
<br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH080]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_80&diff=6921Glycoside Hydrolase Family 802011-07-12T20:32:50Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH80'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|not determined<br />
|-<br />
|'''Active site residues'''<br />
|inferred<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH80.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
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>.<br />
<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 stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation.<br />
<br />
== References ==<br />
<biblio><br />
#Park1999 pmid=10542164<br />
#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.<br />
#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.<br />
<br />
<br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH080]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_80&diff=6920Glycoside Hydrolase Family 802011-07-12T20:29:30Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH80'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|not determined<br />
|-<br />
|'''Active site residues'''<br />
|inferred<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH80.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 80 include bacterial proteins. The were characterized from proteobacteria <cite>Park1999</cite> of from species belonging to the Bacteroidetes/Chlorobi group <cite>Matsuda2001 Yi2004</cite>.<br />
<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 stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation.<br />
<br />
== References ==<br />
<biblio><br />
#Park1999 pmid=10542164<br />
#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.<br />
#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.<br />
<br />
<br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH080]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_80&diff=6919Glycoside Hydrolase Family 802011-07-12T20:28:13Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH80'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|not determined<br />
|-<br />
|'''Active site residues'''<br />
|inferred<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH80.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 80 include bacterial proteins. The were characterized from proteobacteria <cite>Park1999</cite> of from species belonging to the Bacteroidetes/Chlorobi group <cite>Matsuda 2001 Yi2004</cite>.<br />
<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 stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation .<br />
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation.<br />
<br />
== References ==<br />
<biblio><br />
#Park1999 pmid=10542164<br />
#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.<br />
#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.<br />
<br />
<br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH080]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_80&diff=6918Glycoside Hydrolase Family 802011-07-12T20:26:28Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH80'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|not determined<br />
|-<br />
|'''Active site residues'''<br />
|inferred<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH80.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 80 include bacterial proteins. The were characterized from proteobacteria <cite>Park1999</cite> of from species belonging to the Bacteroidetes/Chlorobi group <cite>Matsuda 2001 Yi2004</cite>.<br />
<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 stereochemistry 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>Sinnott1990</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>StickWilliams</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Park1999 pmid=10542164<br />
#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.<br />
#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.<br />
<br />
#StickWilliams isbn=978-0-240-52118-3<br />
#Sinnott1990 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 />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH080]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_80&diff=6917Glycoside Hydrolase Family 802011-07-12T19:50:54Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH80'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH80.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><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>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</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 stereochemistry 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>Sinnott1990</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>StickWilliams</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Comfort2007 pmid=17323919<br />
#He1999 pmid=9312086<br />
#StickWilliams isbn=978-0-240-52118-3<br />
#Sinnott1990 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 />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH080]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_75&diff=6866Glycoside Hydrolase Family 752011-06-03T20:36:54Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH75'''<br />
|-<br />
|'''Clan''' <br />
|Not assigned<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Inferred<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH75.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 75 include both eukaryotic (essentially fungal) and prokaryotic proteins. They have so far been characterized only from filamentous fungi. They are beta-1,4-chitosanases with endo-splitting activity <cite>Shimosaka1993 Cheng2000</cite>. The analysis of the final product of hydrolysis of partially ''N''-deacetylated chitosan by the GH75 chitosanase from ''Aspergillus fumigatus'' suggests that this enzyme cleaves preferentially GlcN-GlcN and GlcNAc-GlcN links in the polysaccharide chain <cite>Cheng2006</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes are classified as inverting enzymes. This has been shown by <sup>1</sup>H NMR for the enzyme from ''Aspergillus fumigatus'' using chitosan as substrate <cite>Cheng2006</cite>.<br />
<br />
<br />
<br />
== Catalytic Residues ==<br />
A site-directed mutagenesis study performed on the enzyme from ''Fusarium solani'' (expressed as a recombinant protein in ''Saccharomyces cerevisiae'') showed that Asp175 and Glu188 are essential for catalysis <cite>Shimosaka2005</cite>. This was confirmed by a study on the chitosanase from ''Aspergillus fumigatus'' (expressed as a recombinant protein in ''Escherichia coli'') showing that the corresponding residues Asp160 and Glu169 are essential for catalysis <cite>Cheng2006</cite>. Both residues are strictly conserved among eukaryotic and prokaryotic GH75 family members.<br />
<br />
<br />
== Three-dimensional structures ==<br />
No three-dimensional structure has been solved for this family.<br />
<br />
<br />
<br />
== Family Firsts ==<br />
;First primary structure determination: Chitosanase from ''Fusarium solani'' f. sp. ''phaseoli'' <cite>Shimosaka1996</cite>.<br />
;First stereochemistry determination: Chitosanase from ''Aspergillus fumigatus'' <cite>Cheng2006</cite>.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet determined.<br />
<br />
== References ==<br />
<biblio><br />
#Shimosaka1993 Shimosaka M, Nogawa M, Ohno Y, and Okazaki M. Chitosanase from the pathogenic fungus, ''Fusarium solani'' f.sp. ''phaseoli'' - purification and some properties. Biosci. Biotech. Biochem. 1993 57, 231-235.<br />
#Cheng2000 pmid=11115392<br />
#Cheng2006 pmid=16330537<br />
#Shimosaka1996 Shimosaka M, Kumehara M, Zhang X-Y, Nogawa M, and Okazaki M. Cloning and characterization of a chitosanase gene from the plant pathogenic fungus Fusarium solani. J. Ferment. Bioeng. 1996 82, 426-431.<br />
#Shimosaka2005 pmid=16384794<br />
<br />
<br />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH075]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_75&diff=6865Glycoside Hydrolase Family 752011-06-03T20:17:09Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH75'''<br />
|-<br />
|'''Clan''' <br />
|Not assigned<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Inferred<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH75.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 75 include both eukaryotic (essentially fungal) and prokaryotic proteins. They have so far been characterized only from filamentous fungi. They are primarily of beta-1,4-chitosanases with endo-splitting activity <cite>Shimosaka1993 Cheng2000</cite>. The analysis of the final product of hydrolysis of partially ''N''-deacetylated chitosan by the GH75 chitosanase from ''Aspergillus fumigatus'' suggests that this enzyme cleaves preferentially GlcN-GlcN and GlcNAc-GlcN links in the polysaccharide chain <cite>Cheng2006</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes are classified as inverting enzymes. This has been shown by <sup>1</sup>H NMR for the enzyme from ''Aspergillus fumigatus'' using chitosan as substrate <cite>Cheng2006</cite>.<br />
<br />
<br />
<br />
== Catalytic Residues ==<br />
A site-directed mutagenesis study performed on the enzyme from ''Fusarium solani'' (expressed as a recombinant protein in ''Saccharomyces cerevisiae'') showed that Asp175 and Glu188 are essential for catalysis <cite>Shimosaka2005</cite>. This was confirmed by a study on the chitosanase from ''Aspergillus fumigatus'' (expressed as a recombinant protein in ''Escherichia coli'') showing that the corresponding residues Asp160 and Glu169 are essential for catalysis <cite>Cheng2006</cite>. Both residues are strictly conserved among eukaryotic and prokaryotic GH75 family members.<br />
<br />
<br />
== Three-dimensional structures ==<br />
No three-dimensional structure has been solved for this family.<br />
<br />
<br />
<br />
== Family Firsts ==<br />
;First primary structure determination: Chitosanase from ''Fusarium solani'' f. sp. ''phaseoli'' <cite>Shimosaka1996</cite>.<br />
;First stereochemistry determination: Chitosanase from ''Aspergillus fumigatus'' <cite>Cheng2006</cite>.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet determined.<br />
<br />
== References ==<br />
<biblio><br />
#Shimosaka1993 Shimosaka M, Nogawa M, Ohno Y, and Okazaki M. Chitosanase from the pathogenic fungus, ''Fusarium solani'' f.sp. ''phaseoli'' - purification and some properties. Biosci. Biotech. Biochem. 1993 57, 231-235.<br />
#Cheng2000 pmid=11115392<br />
#Cheng2006 pmid=16330537<br />
#Shimosaka1996 Shimosaka M, Kumehara M, Zhang X-Y, Nogawa M, and Okazaki M. Cloning and characterization of a chitosanase gene from the plant pathogenic fungus Fusarium solani. J. Ferment. Bioeng. 1996 82, 426-431.<br />
#Shimosaka2005 pmid=16384794<br />
<br />
<br />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH075]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_75&diff=6864Glycoside Hydrolase Family 752011-06-03T20:15:08Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH75'''<br />
|-<br />
|'''Clan''' <br />
|Not assigned<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Inferred<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH75.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 75 include both eukaryotic (essentially fungal) and prokaryotic proteins. They have so far been characterized only from filamentous fungi. They are primarily of beta-1,4-chitosanases with endo-splitting activity <cite>Shimosaka1993 Cheng2000</cite>. The analysis of the final product of hydrolysis of partially ''N''-deacetylated chitosan by the GH75 chitosanase from ''Aspergillus fumigatus'' suggests that this enzyme cleaves preferentially GlcN-GlcN and GlcNAc-GlcN links in the polysaccharide chain <cite>Cheng2006</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes are classified as inverting enzymes. This has been shown by <sup>1</sup>H NMR for the enzyme from ''Aspergillus fumigatus'' using chitosan as substrate <cite>Cheng2006</cite>.<br />
<br />
<br />
<br />
== Catalytic Residues ==<br />
A site-directed mutagenesis study performed on the enzyme from ''Fusarium solani'' (expressed as a recombinant protein in ''Saccharomyces cerevisiae'') showed that Asp175 and Glu188 are essential for catalysis <cite>Shimosaka2005</cite>. This was confirmed by a study on the chitosanase from ''Aspergillus fumigatus'' (expressed as a recombinant protein in ''Escherichia coli'') showing that the corresponding residues Asp160 and Glu169 are essential for catalysis <cite>Cheng2006</cite>. Both residues are strictly conserved among eukaryotic and prokaryotic GH75 family members<br />
<br />
<br />
== Three-dimensional structures ==<br />
No three-dimensional structure has been solved for this family.<br />
<br />
<br />
<br />
== Family Firsts ==<br />
;First primary structure determination: Chitosanase from ''Fusarium solani'' f. sp. ''phaseoli'' <cite>Shimosaka1996</cite>.<br />
;First stereochemistry determination: Chitosanase from ''Aspergillus fumigatus'' <cite>Cheng2006</cite>.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet determined.<br />
<br />
== References ==<br />
<biblio><br />
#Shimosaka1993 Shimosaka M, Nogawa M, Ohno Y, and Okazaki M. Chitosanase from the pathogenic fungus, ''Fusarium solani'' f.sp. ''phaseoli'' - purification and some properties. Biosci. Biotech. Biochem. 1993 57, 231-235.<br />
#Cheng2000 pmid=11115392<br />
#Cheng2006 pmid=16330537<br />
#Shimosaka1996 Shimosaka M, Kumehara M, Zhang X-Y, Nogawa M, and Okazaki M. Cloning and characterization of a chitosanase gene from the plant pathogenic fungus Fusarium solani. J. Ferment. Bioeng. 1996 82, 426-431.<br />
#Shimosaka2005 pmid=16384794<br />
<br />
<br />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH075]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_75&diff=6863Glycoside Hydrolase Family 752011-06-03T19:56:24Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH75'''<br />
|-<br />
|'''Clan''' <br />
|Not assigned<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Inferred<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH75.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 75 include both eukaryotic (essentially fungal) and prokaryotic proteins. They have so far been characterized only from filamentous fungi. They are primarily of beta-1,4-chitosanases with endo-splitting activity <cite>Shimosaka1993 Cheng2000</cite>. The analysis of the final product of hydrolysis of partially ''N''-deacetylated chitosan by the GH75 chitosanase from ''Aspergillus fumigatus'' suggests that this enzyme cleaves preferentially GlcN-GlcN and GlcNAc-GlcN links in the polysaccharide chain <cite>Cheng2006</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes are classified as inverting enzymes. This has been shown by <sup>1</sup>H NMR for the enzyme from ''Aspergillus fumigatus'' using chitosan as substrate <cite>Cheng2006</cite>.<br />
<br />
<br />
<br />
== Catalytic Residues ==<br />
A site-directed mutagenesis study performed on the enzyme from ''Aspergillus fumigatus'' expressed as a recombinant protein in ''Escherichia coli'' showed that Asp160 and Glu169 are essential for catalysis <cite>Cheng2006</cite>. Both residues are strictly conserved among eukaryotic and prokaryotic GH75 family members<br />
<br />
<br />
== Three-dimensional structures ==<br />
No three-dimensional structure has been solved for this family.<br />
<br />
<br />
<br />
== Family Firsts ==<br />
;First primary structure determination: Chitosanase from ''Fusarium solani'' f. sp. ''phaseoli'' <cite>Shimosaka1996</cite>.<br />
;First stereochemistry determination: Chitosanase from ''Aspergillus fumigatus'' <cite>Cheng2006</cite>.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet determined.<br />
<br />
== References ==<br />
<biblio><br />
#Shimosaka1993 Shimosaka M, Nogawa M, Ohno Y, and Okazaki M. Chitosanase from the pathogenic fungus, ''Fusarium solani'' f.sp. ''phaseoli'' - purification and some properties. Biosci. Biotech. Biochem. 1993 57, 231-235.<br />
#Cheng2000 pmid=11115392<br />
#Cheng2006 pmid=16330537<br />
#Shimosaka1996 Shimosaka M, Kumehara M, Zhang X-Y, Nogawa M, and Okazaki M. Cloning and characterization of a chitosanase gene from the plant pathogenic fungus Fusarium solani. J. Ferment. Bioeng. 1996 82, 426-431.<br />
<br />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH075]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_75&diff=6862Glycoside Hydrolase Family 752011-06-03T19:53:07Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH75'''<br />
|-<br />
|'''Clan''' <br />
|Not assigned<br />
|-<br />
|'''Mechanism'''<br />
|Inverting<br />
|-<br />
|'''Active site residues'''<br />
|Inferred<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH75.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 75 include both eukaryotic (essentially fungal) and prokaryotic proteins. They have so far been characterized only from filamentous fungi. They are primarily of beta-1,4-chitosanases with endo-splitting activity <cite>Shimosaka1993 Cheng2000</cite>. The analysis of the final product of hydrolysis of partially ''N''-deacetylated chitosan by the GH75 chitosanase from ''Aspergillus fumigatus'' suggests that this enzyme cleaves preferentially GlcN-GlcN and GlcNAc-GlcN links in the polysaccharide chain <cite>Cheng2006</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes are classified as inverting enzymes. This has been shown by <sup>1</sup>H NMR for the enzyme from ''Aspergillus fumigatus'' using chitosan as substrate <cite>Cheng2006</cite>.<br />
<br />
<br />
<br />
== Catalytic Residues ==<br />
A site-directed mutagenesis study performed on the enzyme from ''Aspergillus fumigatus'' expressed as a recombinant protein in ''Escherichia coli'' showed that Asp160 and Glu169 are essential for catalysis <cite>Cheng2006</cite>. Both residues are strictly conserved among eukaryotic and prokaryotic GH75 family members<br />
<br />
<br />
== Three-dimensional structures ==<br />
No three-dimensional structure has been solved for this family.<br />
<br />
<br />
<br />
== Family Firsts ==<br />
;First primary structure determination: Chitosanase from ''Fusarium solani'' f. sp. ''phaseoli'' <Shimosaka1996>.<br />
;First stereochemistry determination: Chitosanase from ''Aspergillus fumigatus'' <cite>Cheng2006</cite>.<br />
;First catalytic nucleophile identification: Not yet identified.<br />
;First general acid/base residue identification: Not yet identified.<br />
;First 3-D structure: Not yet determined.<br />
<br />
== References ==<br />
<biblio><br />
#Shimosaka1993 Shimosaka M, Nogawa M, Ohno Y, and Okazaki M. Chitosanase from the pathogenic fungus, ''Fusarium solani'' f.sp. ''phaseoli'' - purification and some properties. Biosci. Biotech. Biochem. 1993 57, 231-235.<br />
#Cheng2000 pmid=11115392<br />
#Cheng2006 pmid=16330537<br />
#Shimosaka1996 Shimosaka M, Kumehara M, Zhang X-Y, Nogawa M, and Okazaki M. Cloning and characterization of a chitosanase gene from the plant pathogenic fungus Fusarium solani. J. Ferment. Bioeng. 1996 82, 426-431.<br />
<br />
<br />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH075]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_75&diff=6861Glycoside Hydrolase Family 752011-06-03T19:17:45Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH75'''<br />
|-<br />
|'''Clan''' <br />
|Not assigned<br />
|-<br />
|'''Mechanism'''<br />
|inverting<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH75.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 75 include both eukaryotic (essentially fungal) and prokaryotic proteins. They have so far been characterized only from filamentous fungi. They are primarily of beta-1,4-chitosanases with endo-splitting activity <cite>Shimosaka1993 Cheng2000</cite>. The analysis of the final product of hydrolysis of partially ''N''-deacetylated chitosan by the GH75 chitosanase from ''Aspergillus fumigatus'' suggests that this enzyme cleaves preferentially GlcN-GlcN and GlcNAc-GlcN links in the polysaccharide chain <cite>Cheng2006</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes utilize an inverting mechanism as shown by NMR <cite>Cheng2006</cite>.<br />
<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 />
<br />
== Family Firsts ==<br />
;First stereochemistry 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>Sinnott1990</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>StickWilliams</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shimosaka1993 Shimosaka M, Nogawa M, Ohno Y, and Okazaki M. Chitosanase from the pathogenic fungus, ''Fusarium solani'' f.sp. ''phaseoli'' - purification and some properties. Biosci. Biotech. Biochem. 57, 231-235.<br />
#Cheng2000 pmid=11115392<br />
#Cheng2006 pmid=16330537<br />
<br />
<br />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH075]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_75&diff=6860Glycoside Hydrolase Family 752011-06-03T19:02:35Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH75'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH75.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 75 include both eukaryotic (essentially fungal) and prokaryotic proteins. They have so far been characterized only from fimanetous fungi. They are primarily of beta-1,4-chitosanases with endo-splitting activity <cite>Shimosaka1993 Cheng2000</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes utilize an inverting mechanism as shown by NMR <cite>Cheng2006</cite>.<br />
<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 />
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>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry 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>Sinnott1990</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>StickWilliams</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shimosaka1993 Shimosaka M, Nogawa M, Ohno Y, and Okazaki M. Chitosanase from the pathogenic fungus, ''Fusarium solani'' f.sp. ''phaseoli'' - purification and some properties. Biosci. Biotech. Biochem. 57, 231-235.<br />
#Cheng2000 pmid=11115392<br />
#Cheng2006 pmid=16330537<br />
<br />
<br />
#Comfort2007 pmid=17323919<br />
#He1999 pmid=9312086<br />
#StickWilliams isbn=978-0-240-52118-3<br />
#Sinnott1990 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 />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH075]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_75&diff=6859Glycoside Hydrolase Family 752011-06-03T18:58:14Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH75'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH75.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 75 include both eukaryotic (essentially fungal) and prokaryotic proteins. They have so far been characterized only from fimanetous fungi. They are primarily of beta-1,4-chitosanases with endo-splitting activity <cite>Shimosaka1993 Cheng2000</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes utilize an inverting mechanism as shown by NMR <cite>Chend2006</cite>.<br />
<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 />
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>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry 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>Sinnott1990</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>StickWilliams</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shimosaka1993 Shimosaka M, Nogawa M, Ohno Y, and Okazaki M. Chitosanase from the pathogenic fungus, ''Fusarium solani'' f.sp. ''phaseoli'' - purification and some properties. Biosci. Biotech. Biochem. 57, 231-235.<br />
#Cheng2000 pmid=11115392<br />
#Comfort2007 pmid=17323919<br />
#He1999 pmid=9312086<br />
#StickWilliams isbn=978-0-240-52118-3<br />
#Sinnott1990 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 />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH075]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_75&diff=6843Glycoside Hydrolase Family 752011-05-27T21:00:09Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH75'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH75.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 75 are primarily of endo-beta-1,4-chitosanases <cite>Shimosaka1993 Cheng2000</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>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</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 stereochemistry 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>Sinnott1990</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>StickWilliams</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shimosaka1993 Shimosaka M, Nogawa M, Ohno Y, and Okazaki M. Chitosanase from the pathogenic fungus, ''Fusarium solani'' f.sp. ''phaseoli'' - purification and some properties. Biosci. Biotech. Biochem. 57, 231-235.<br />
#Cheng2000 pmid=11115392<br />
#Comfort2007 pmid=17323919<br />
#He1999 pmid=9312086<br />
#StickWilliams isbn=978-0-240-52118-3<br />
#Sinnott1990 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 />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH075]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_75&diff=6842Glycoside Hydrolase Family 752011-05-27T20:56:24Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH75'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH75.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 75 are primarily of endo-beta-1,4-chitosanases <cite>Shimosaka1993 Cheng2000</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>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</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 stereochemistry 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>Sinnott1990</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>StickWilliams</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shimosaka1993 Shimosaka M, Nogawa M, Ohno Y, and Okazaki M. Chitosanase from the pathogenic fungus, ''Fusarium solani'' f.sp. ''phaseoli'' - purification and some properties. Biosci. Biotech. Biochem. 57, 231-235.<br />
#Comfort2007 pmid=17323919<br />
#He1999 pmid=9312086<br />
#StickWilliams isbn=978-0-240-52118-3<br />
#Sinnott1990 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 />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH075]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_75&diff=6841Glycoside Hydrolase Family 752011-05-27T20:47:01Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH75'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH75.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 75 are primarily of endo-beta-1,4-chitosanases <cite>Shimosaka1993 Cheng2000</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>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</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 stereochemistry 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>Sinnott1990</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>StickWilliams</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Shimosaka1993<br />
#Comfort2007 pmid=17323919<br />
#He1999 pmid=9312086<br />
#StickWilliams isbn=978-0-240-52118-3<br />
#Sinnott1990 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 />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH075]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_75&diff=6840Glycoside Hydrolase Family 752011-05-27T20:39:16Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: <br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH75'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH75.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><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>StickWilliams</cite>. References that are not in PubMed can be typed in by hand <cite>Sinnott1990</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 stereochemistry 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>Sinnott1990</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>StickWilliams</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Comfort2007 pmid=17323919<br />
#He1999 pmid=9312086<br />
#StickWilliams isbn=978-0-240-52118-3<br />
#Sinnott1990 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 />
</biblio><br />
<br />
<br />
<br />
[[Category:Glycoside Hydrolase Families|GH075]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=4123Glycoside Hydrolase Family 462010-02-23T21:57:31Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^; ^^^Marie-Ève Lacombe-Harvey^^^<br />
<br />
<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH46'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
[[Glycoside hydrolases]] of family 46 are essentially all ''endo''-beta-1,4-chitosanases (EC [{{EClink}}3.2.1.132 3.2.1.132]) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits in chitosan, all the enzymes examined for their cleavage specificity acted upon the GlcN-GlcN links. In addition, the chitosanase from ''Bacillus circulans'' MH-K1 recognized also GlcN-GlcNAc links <cite>Mitsutomi1996</cite>, while the chitosanase from ''Streptomyces'' sp. N174 recognized the GlcNAc-GlcN links <cite>Fukamizo1995</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes utilize an [[inverting]] mechanism, as shown by NMR <cite>Fukamizo1995</cite>.<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues have been identified by site-directed mutagenesis and crystallography in the chitosanase from Streptomyces sp. N174. The [[general acid]] residue is Glu22 in the sequence SSA<u>'''E'''</u>NSS, while Asp40 (DIG<u>'''D'''</u>GRG) is the [[general base]] residue <cite>Boucher1995 Marcotte1996</cite>. The latter could activate the nucleophilic water molecule with assistance from residue Thr45 (RGY<u>'''T'''</u>GGI) <cite>Lacombe-Harvey2009</cite>. Analysis of sequence alignments as well as crystallographic evidence showed that the same function is played by residues Glu37 (in the sequence NKP'''<u>E</u>'''QDD) , Asp55 (DIE<u>'''D'''</u>ERG) and Thr60 (RGY'''<u>T</u>'''IGL) in the chitosanase from ''Bacillus circulans'' MH-K1 <cite>Saito1999</cite>.<br />
<br />
== Three-dimensional structures ==<br />
[[File:csn_entire_5a.png|200px|thumb|right|3D structure of the chitosanase from ''Streptomyces'' sp. N174]] <br />
Two structures have been solved using X-ray crystallography, for the chitosanases from Streptomyces sp. N174 <cite>Marcotte1996</cite> and from Bacillus circulans MH-K1 (wild-type enzyme <cite>Saito1999</cite> and mutant K218P <cite>Fukamizo2005</cite>. These enzymes have essentially an alpha-helical fold, with two globular domains separated by the active site cleft for substrate binding. The cleft is bordered on the upper face by a three-stranded beta-sheet. The structure of GH46 enzymes is similar to the 3D fold of the well studied lysozyme of bacteriophage T4 of ''Escherichia coli'' belonging to family GH24 <cite>Marcotte1996</cite> and, to some extent, to the structures of lysozymes from families GH22, GH23 as well the chitinases from family GH19 <cite>Monzingo1996</cite>. These five families are sometimes grouped in the "lysozyme superfamily" <cite>Holm1994 Lacombe-Harvey2009</cite>. <br />
The crystal structures, completed by site-directed mutagenesis have also revealed several residues involved in substrate binding <cite>Marcotte1996 Fukamizo2005 Tremblay2001 Katsumi2005</cite>. For the chitosanase from ''Streptomyces'' sp N174, the mode of binding of a GlcN hexasaccharide was established as being in conformity with a symmetrical 3+3 model, based on the analysis of products of hydrolysis <cite>Tremblay2001</cite>. <br />
<br />
== Family Firsts ==<br />
;First primary sequence determination: Chitosanase from ''Bacillus circulans'' MH-K1 <cite>Ando1992</cite>.<br />
;First sterochemistry determination: Chitosanase from ''Streptomyces'' sp. N174 by NMR <cite>Fukamizo1995</cite>.<br />
;First [[general base]] residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.<br />
;First [[general acid]] residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.<br />
;First 3-D structure: Chitosanase from ''Streptomyces'' sp. N174 by X-ray crystallography <cite>Marcotte1996</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.<br />
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, WA., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.<br />
#Mitsutomi1996 Mitsutomi, M., Ueda, M., Arai, M., Ando, A., Watanabe, T. (1996) Action patterns of microbial chitinases and chitosanases on partially ''N''-acetylated chitosan. Chitin Enzymology, vol. 2, pp 273-284.<br />
#Fukamizo1995 pmid=7487871<br />
#Boucher1995 pmid=8537367<br />
#Lacombe-Harvey2009 pmid=19143844<br />
#Saito1999 pmid=10521473<br />
#Marcotte1996 pmid=8564542<br />
#Fukamizo2005 pmid=16272568<br />
#Monzingo1996 pmid=8564539<br />
#Holm1994 pmid=8119396<br />
#Tremblay2001 pmid=11686931<br />
#Katsumi2005 pmid=16288718<br />
#Ando1992 Ando, A., Noguchi, K., Yanagi, M., Shinoyama, H., Kagawa, Y., Hirata, H., Yabuki, M., Fujii, T. (1992) Primary structure of chitosanase produced by ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 38:135-144.<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=3717Glycoside Hydrolase Family 462010-02-10T16:21:26Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH46'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 46 are essentially ''endo''-beta-1,4-chitosanases (EC [{{EClink}}3.2.1.132 3.2.1.132]) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits in chitosan, all the enzymes examined for their cleavage specificity recognized productively the GlcN-GlcN links. In addition, the chitosanase from ''Bacillus circulans'' MH-K1 recognized also GlcN-GlcNAc links <cite>Mitsutomi1996</cite>, while the chitosanase from ''Streptomyces'' sp. N174 recognized the GlcNAc-GlcN links <cite>Fukamizo1995</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes utilize an inverting mechanism, as shown by NMR <cite>Fukamizo1995</cite>.<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues have been identified by site-directed mutagenesis and crystallography in the chitosanase from Streptomyces sp. N174. The general acid residue is Glu22 in the sequence SSA<u>'''E'''</u>NSS, while Asp40 (DIG<u>'''D'''</u>GRG) is the general base residue <cite>Boucher1995 Marcotte1996</cite>. The latter could activate the nucleophilic water molecule with assistance from residue Thr45 (RGY<u>'''T'''</u>GGI) <cite>Lacombe-Harvey2009</cite>. Analysis of sequence alignments as well as crystallographic evidence showed that the same function is played by residues Glu37 (in the sequence NKP'''<u>E</u>'''QDD) , Asp55 (DIE<u>'''D'''</u>ERG) and Thr60 (RGY'''<u>T</u>'''IGL) in the chitosanase from ''Bacillus circulans'' MH-K1 <cite>Saito1999</cite>.<br />
<br />
== Three-dimensional structures ==<br />
Two structures have been solved using X-ray crystallography, for the chitosanases from Streptomyces sp. N174 <cite>Marcotte1996</cite> and from Bacillus circulans MH-K1 (wild-type enzyme <cite>Saito1999</cite> and mutant K218P <cite>Fukamizo2005</cite>. These enzymes have essentially an alpha-helical fold, with two globular domains separated by the active site cleft for substrate binding. The cleft is bordered on the upper face by a three-stranded beta-sheet. The structure of GH46 enzymes is similar to the 3D fold of the well studied lysozyme of bacteriophage T4 of ''Escherichia coli'' belonging to family GH24 <cite>Marcotte1996</cite> and, to some extent, to the structures of lysozymes from families GH22, GH23 as well the chitinases from family GH19 <cite>Monzingo1996</cite>. These five families are sometimes grouped in the "lysozyme superfamily" <cite>Holm1994 Lacombe-Harvey2009</cite>. <br />
The crystal structures, completed by site-directed mutagenesis have also revealed several residues involved in substrate binding <cite>Marcotte1996 Fukamizo2005 Tremblay2001 Katsumi2005</cite>. For the chitosanase from ''Streptomyces'' sp N174, the mode of binding of a GlcN hexasaccharide was established as being in conformity with a symmetrical 3+3 model, based on the analysis of products of hydrolysis <cite>Tremblay2001</cite>. <br />
<br />
== Family Firsts ==<br />
;First primary sequence determination: Chitosanase from ''Bacillus circulans'' MH-K1 <cite>Ando1992</cite>.<br />
;First sterochemistry determination: Chitosanase from ''Streptomyces'' sp. N174 by NMR <cite>Fukamizo1995</cite>.<br />
;First general base residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.<br />
;First general acid residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.<br />
;First 3-D structure: Chitosanase from ''Streptomyces'' sp. N174 by X-ray crystallography <cite>Marcotte1996</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.<br />
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, WA., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.<br />
#Mitsutomi1996 Mitsutomi, M., Ueda, M., Arai, M., Ando, A., Watanabe, T. (1996) Action patterns of microbial chitinases and chitosanases on partially ''N''-acetylated chitosan. Chitin Enzymology, vol. 2, pp 273-284.<br />
#Fukamizo1995 pmid=7487871<br />
#Boucher1995 pmid=8537367<br />
#Lacombe-Harvey2009 pmid=19143844<br />
#Saito1999 pmid=10521473<br />
#Marcotte1996 pmid=8564542<br />
#Fukamizo2005 pmid=16272568<br />
#Monzingo1996 pmid=8564539<br />
#Holm1994 pmid=8119396<br />
#Tremblay2001 pmid=11686931<br />
#Katsumi2005 pmid=16288718<br />
#Ando1992 Ando, A., Noguchi, K., Yanagi, M., Shinoyama, H., Kagawa, Y., Hirata, H., Yabuki, M., Fujii, T. (1992) Primary structure of chitosanase produced by ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 38:135-144.<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=3716Glycoside Hydrolase Family 462010-02-10T16:12:20Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{CuratorApproved}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 46 are essentially ''endo''-beta-1,4-chitosanases (EC [{{EClink}}3.2.1.132 3.2.1.132]) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits in chitosan, all the enzymes examined for their cleavage specificity recognized productively the GlcN-GlcN links. In addition, the chitosanase from ''Bacillus circulans'' MH-K1 recognized also GlcN-GlcNAc links <cite>Mitsutomi1996</cite>, while the chitosanase from ''Streptomyces'' sp. N174 recognized the GlcNAc-GlcN links <cite>Fukamizo1995</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes utilize an inverting mechanism, as shown by NMR <cite>Fukamizo1995</cite>.<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues have been identified by site-directed mutagenesis and crystallography in the chitosanase from Streptomyces sp. N174. The general acid residue is Glu22 in the sequence SSA<u>'''E'''</u>NSS, while Asp40 (DIG<u>'''D'''</u>GRG) is the general base residue <cite>Boucher1995 Marcotte1996</cite>. The latter could activate the nucleophilic water molecule with assistance from residue Thr45 (RGY<u>'''T'''</u>GGI) <cite>Lacombe-Harvey2009</cite>. Analysis of sequence alignments as well as crystallographic evidence showed that the same function is played by residues Glu37 (in the sequence NKP'''<u>E</u>'''QDD) , Asp55 (DIE<u>'''D'''</u>ERG) and Thr60 (RGY'''<u>T</u>'''IGL) in the chitosanase from ''Bacillus circulans'' MH-K1 <cite>Saito1999</cite>.<br />
<br />
== Three-dimensional structures ==<br />
Two structures have been solved using X-ray crystallography, for the chitosanases from Streptomyces sp. N174 <cite>Marcotte1996</cite> and from Bacillus circulans MH-K1 (wild-type enzyme <cite>Saito1999</cite> and mutant K218P <cite>Fukamizo2005</cite>. These enzymes have essentially an alpha-helical fold, with two globular domains separated by the active site cleft for substrate binding. The cleft is bordered on the upper face by a three-stranded beta-sheet. The structure of GH46 enzymes is similar to the 3D fold of the well studied lysozyme of bacteriophage T4 of ''Escherichia coli'' belonging to family GH24 <cite>Marcotte1996</cite> and, to some extent, to the structures of lysozymes from families GH22, GH23 as well the chitinases from family GH19 <cite>Monzingo1996</cite>. These five families are sometimes grouped in the "lysozyme superfamily" <cite>Holm1994 Lacombe-Harvey2009</cite>. <br />
The crystal structures, completed by site-directed mutagenesis have also revealed several residues involved in substrate binding <cite>Marcotte1996 Fukamizo2005 Tremblay2001 Katsumi2005</cite>. For the chitosanase from ''Streptomyces'' sp N174, the mode of binding of a GlcN hexasaccharide was established as being in conformity with a symmetrical 3+3 model, based on the analysis of products of hydrolysis <cite>Tremblay2001</cite>. <br />
<br />
== Family Firsts ==<br />
;First primary sequence determination: Chitosanase from ''Bacillus circulans'' MH-K1 <cite>Ando1992</cite>.<br />
;First sterochemistry determination: Chitosanase from ''Streptomyces'' sp. N174 by NMR <cite>Fukamizo1995</cite>.<br />
;First general base residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.<br />
;First general acid residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.<br />
;First 3-D structure: Chitosanase from ''Streptomyces'' sp. N174 by X-ray crystallography <cite>Marcotte1996</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.<br />
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, WA., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.<br />
#Mitsutomi1996 Mitsutomi, M., Ueda, M., Arai, M., Ando, A., Watanabe, T. (1996) Action patterns of microbial chitinases and chitosanases on partially ''N''-acetylated chitosan. Chitin Enzymology, vol. 2, pp 273-284.<br />
#Fukamizo1995 pmid=7487871<br />
#Boucher1995 pmid=8537367<br />
#Lacombe-Harvey2009 pmid=19143844<br />
#Saito1999 pmid=10521473<br />
#Marcotte1996 pmid=8564542<br />
#Fukamizo2005 pmid=16272568<br />
#Monzingo1996 pmid=8564539<br />
#Holm1994 pmid=8119396<br />
#Tremblay2001 pmid=11686931<br />
#Katsumi2005 pmid=16288718<br />
#Ando1992 Ando, A., Noguchi, K., Yanagi, M., Shinoyama, H., Kagawa, Y., Hirata, H., Yabuki, M., Fujii, T. (1992) Primary structure of chitosanase produced by ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 38:135-144.<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=3674Glycoside Hydrolase Family 462010-02-09T15:12:47Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 46 are essentially ''endo''-beta-1,4-chitosanases (EC [{{EClink}}3.2.1.132 3.2.1.132]) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits in chitosan, all the enzymes examined for their cleavage specificity recognized productively the GlcN-GlcN links. In addition, the chitosanase from ''Bacillus circulans'' MH-K1 recognized also GlcN-GlcNAc links <cite>Mitsutomi1996</cite>, while the chitosanase from ''Streptomyces'' sp. N174 recognized the GlcNAc-GlcN links <cite>Fukamizo1995</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes utilize an inverting mechanism, as shown by NMR <cite>Fukamizo1995</cite>.<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues have been identified by site-directed mutagenesis and crystallography in the chitosanase from Streptomyces sp. N174. The general acid residue is Glu22 in the sequence SSA<u>'''E'''</u>NSS, while Asp40 (DIG<u>'''D'''</u>GRG) is the general base residue <cite>Boucher1995 Marcotte1996</cite>. The latter could activate the nucleophilic water molecule with assistance from residue Thr45 (RGY<u>'''T'''</u>GGI) <cite>Lacombe-Harvey2009</cite>. Analysis of sequence alignments as well as crystallographic evidence showed that the same function is played by residues Glu37 (in the sequence NKP'''<u>E</u>'''QDD) , Asp55 (DIE<u>'''D'''</u>ERG) and Thr60 (RGY'''<u>T</u>'''IGL) in the chitosanase from ''Bacillus circulans'' MH-K1 <cite>Saito1999</cite>.<br />
<br />
== Three-dimensional structures ==<br />
Two structures have been solved using X-ray crystallography, for the chitosanases from Streptomyces sp. N174 <cite>Marcotte1996</cite> and from Bacillus circulans MH-K1 (wild-type enzyme <cite>Saito1999</cite> and mutant K218P <cite>Fukamizo2005</cite>. These enzymes have essentially an alpha-helical fold, with two globular domains separated by the active site cleft for substrate binding. The cleft is bordered on the upper face by a three-stranded beta-sheet. The structure of GH46 enzymes is similar to the 3D fold of the well studied lysozyme of bacteriophage T4 of ''Escherichia coli'' belonging to family GH24 <cite>Marcotte1996</cite> and, to some extent, to the structures of lysozymes from families GH22, GH23 as well the chitinases from family GH19 <cite>Monzingo1996</cite>. These five families are sometimes grouped in the "lysozyme superfamily" <cite>Holm1994 Lacombe-Harvey2009</cite>. <br />
The crystal structures, completed by site-directed mutagenesis have also revealed several residues involved in substrate binding <cite>Marcotte1996 Fukamizo2005 Tremblay2001 Katsumi2005</cite>. For the chitosanase from ''Streptomyces'' sp N174, the mode of binding of a GlcN hexasaccharide was established as being in conformity with a symmetrical 3+3 model, based on the analysis of products of hydrolysis <cite>Tremblay2001</cite>. <br />
<br />
== Family Firsts ==<br />
;First primary sequence determination: Chitosanase from ''Bacillus circulans'' MH-K1 <cite>Ando1992</cite>.<br />
;First sterochemistry determination: Chitosanase from ''Streptomyces'' sp. N174 by NMR <cite>Fukamizo1995</cite>.<br />
;First general base residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.<br />
;First general acid residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.<br />
;First 3-D structure: Chitosanase from ''Streptomyces'' sp. N174 by X-ray crystallography <cite>Marcotte1996</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.<br />
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, WA., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.<br />
#Mitsutomi1996 Mitsutomi, M., Ueda, M., Arai, M., Ando, A., Watanabe, T. (1996) Action patterns of microbial chitinases and chitosanases on partially ''N''-acetylated chitosan. Chitin Enzymology, vol. 2, pp 273-284.<br />
#Fukamizo1995 pmid=7487871<br />
#Boucher1995 pmid=8537367<br />
#Lacombe-Harvey2009 pmid=19143844<br />
#Saito1999 pmid=10521473<br />
#Marcotte1996 pmid=8564542<br />
#Fukamizo2005 pmid=16272568<br />
#Monzingo1996 pmid=8564539<br />
#Holm1994 pmid=8119396<br />
#Tremblay2001 pmid=11686931<br />
#Katsumi2005 pmid=16288718<br />
#Ando1992 Ando, A., Noguchi, K., Yanagi, M., Shinoyama, H., Kagawa, Y., Hirata, H., Yabuki, M., Fujii, T. (1992) Primary structure of chitosanase produced by ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 38:135-144.<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=3673Glycoside Hydrolase Family 462010-02-09T15:08:20Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 46 are essentially ''endo''-beta-1,4-chitosanases (EC [{{EClink}}3.2.1.132 3.2.1.132]) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits in chitosan, all the enzymes examined for their cleavage specificity recognized productively the GlcN-GlcN links. In addition, the chitosanase from ''Bacillus circulans'' MH-K1 recognized also GlcN-GlcNAc links <cite>Mitsutomi1996</cite>, while the chitosanase from ''Streptomyces'' sp. N174 recognized the GlcNAc-GlcN links <cite>Fukamizo1995</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes utilize an inverting mechanism, as shown by NMR <cite>Fukamizo1995</cite>.<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues have been identified by site-directed mutagenesis and crystallography in the chitosanase from Streptomyces sp. N174. The general acid residue is Glu22 in the sequence SSA<u>'''E'''</u>NSS, while Asp40 (DIG<u>'''D'''</u>GRG) is the general base residue <cite>Boucher1995 Marcotte1996</cite>. The latter could activate the nucleophilic water molecule with assistance from residue Thr45 (RGY<u>'''T'''</u>GGI) <cite>Lacombe-Harvey2009</cite>. Analysis of sequence alignments as well as crystallographic evidence showed that the same function is played by residues Glu37 (in the sequence NKP'''<u>E</u>'''QDD) , Asp55 (DIE<u>'''D'''</u>ERG) and Thr60 (RGY'''<u>T</u>'''IGL) in the chitosanase from ''Bacillus circulans'' MH-K1 <cite>Saito1999</cite>.<br />
<br />
== Three-dimensional structures ==<br />
Two structures have been solved using X-ray crystallography, for the chitosanases from Streptomyces sp. N174 <cite>Marcotte1996</cite> and from Bacillus circulans MH-K1 (wild-type enzyme <cite>Saito1999</cite> and mutant K218P <cite>Fukamizo2005</cite>. These enzymes have essentially an alpha-helical fold, with two globular domains separated by the active site cleft for substrate binding. The cleft is bordered on the upper face by a three-stranded beta-sheet. The structure is similar to the 3D fold of the well studied lysozyme of bacteriophage T4 of ''Escherichia coli'' belonging to family GH24 <cite>Marcotte1996</cite> and, to some extent, to the structures of lysozymes from families GH22, GH23 as well the chitinases from family GH19 <cite>Monzingo1996</cite>. These five families are sometimes grouped in the "lysozyme superfamily" <cite>Holm1994 Lacombe-Harvey2009</cite>. <br />
The crystal structures, completed by site-directed mutagenesis have also revealed several residues involved in substrate binding <cite>Marcotte1996 Fukamizo2005 Tremblay2001 Katsumi2005</cite>. For the chitosanase from ''Streptomyces'' sp N174, the mode of binding of a GlcN hexasaccharide was established as being in conformity with a symmetrical 3+3 model, based on the analysis of products of hydrolysis <cite>Tremblay2001</cite>. <br />
<br />
== Family Firsts ==<br />
;First primary sequence determination: Chitosanase from ''Bacillus circulans'' MH-K1 <cite>Ando1992</cite>.<br />
;First sterochemistry determination: Chitosanase from ''Streptomyces'' sp. N174 by NMR <cite>Fukamizo1995</cite>.<br />
;First general base residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.<br />
;First general acid residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.<br />
;First 3-D structure: Chitosanase from ''Streptomyces'' sp. N174 by X-ray crystallography <cite>Marcotte1996</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.<br />
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, WA., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.<br />
#Mitsutomi1996 Mitsutomi, M., Ueda, M., Arai, M., Ando, A., Watanabe, T. (1996) Action patterns of microbial chitinases and chitosanases on partially ''N''-acetylated chitosan. Chitin Enzymology, vol. 2, pp 273-284.<br />
#Fukamizo1995 pmid=7487871<br />
#Boucher1995 pmid=8537367<br />
#Lacombe-Harvey2009 pmid=19143844<br />
#Saito1999 pmid=10521473<br />
#Marcotte1996 pmid=8564542<br />
#Fukamizo2005 pmid=16272568<br />
#Monzingo1996 pmid=8564539<br />
#Holm1994 pmid=8119396<br />
#Tremblay2001 pmid=11686931<br />
#Katsumi2005 pmid=16288718<br />
#Ando1992 Ando, A., Noguchi, K., Yanagi, M., Shinoyama, H., Kagawa, Y., Hirata, H., Yabuki, M., Fujii, T. (1992) Primary structure of chitosanase produced by ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 38:135-144.<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=3666Glycoside Hydrolase Family 462010-02-04T21:21:35Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 46 are essentially ''endo''-beta-1,4-chitosanases (EC 3.2.1.132) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits in chitosan, all the enzymes examined for their cleavage specificity recognized productively the GlcN-GlcN links. In addition, the chitosanase from ''Bacillus circulans'' MH-K1 recognized also GlcN-GlcNAc links <cite>Mitsutomi1996</cite>, while the chitosanase from ''Streptomyces'' sp. N174 recognized the GlcNAc-GlcN links <cite>Fukamizo1995</cite>. <br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes utilize an inverting mechanism, as shown by NMR <cite>Fukamizo1995</cite>.<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues have been identified by site-directed mutagenesis and crystallography in the chitosanase from Streptomyces sp. N174. The general acid residue is Glu22, while Asp40 is the general base residue <cite>Boucher1995 Marcotte1996</cite>. The latter could activate the nucleophilic water molecule with assistance from residue Thr45 <cite>Lacombe-Harvey2009</cite>. Analysis of sequence alignments as well as crystallographic evidence showed that the same function is played by residues Glu37, Asp55 and Thr60 in the chitosanase from ''Bacillus circulans'' MH-K1 <cite>Saito1999</cite>.<br />
<br />
<br />
== Three-dimensional structures ==<br />
Two structures have been solved using X-ray crystallography, for the chitosanases from Streptomyces sp. N174 <cite>Marcotte1996</cite> and from Bacillus circulans MH-K1 (wild-type enzyme <cite>Saito1999</cite> and mutant K218P <cite>Fukamizo2005</cite>. These enzymes have essentially an alpha-helical fold, with two globular domains separated by the active site cleft for substrate binding. The cleft is bordered on the upper face by a three-stranded beta-sheet. The structure is similar to the 3D fold of the well studied lysozyme of bacteriophage T4 of ''Escherichia coli'' belonging to family GH24 <cite>Marcotte1996</cite> and, to some extent, to the structures of lysozymes from families GH22, GH23 as well the chitinases from family GH19 <cite>Monzingo1996</cite>. These five families are sometimes grouped in the "lysozyme superfamily" <cite>Holm1994 Lacombe-Harvey2009</cite>. <br />
The crystal structures, completed by site-directed mutagenesis have also revealed several residues involved in substrate binding <cite>Marcotte1996 Fukamizo2005 Tremblay2001 Katsumi2005</cite>. While a 4+2 model of substrate binding has been initially proposed for a GlcN hexasaccharide <cite>Marcotte1996</cite>, the mode of binding was later established as being in conformity with a 3+3 model, based on the analysis of products of hydrolysis <cite>Tremblay2001</cite>. <br />
<br />
<br />
== Family Firsts ==<br />
;First primary sequence determination: Chitosanase from ''Bacillus circulans'' MH-K1 <cite>Ando1992</cite>.<br />
;First sterochemistry determination: Chitosanase from ''Streptomyces'' sp. N174 by NMR <cite>Fukamizo1995</cite>.<br />
;First catalytic nucleophile identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.<br />
;First general acid/base residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.<br />
;First 3-D structure: Chitosanase from ''Streptomyces'' sp. N174 by X-ray crystallography <cite>Marcotte1996</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.<br />
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, WA., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.<br />
#Mitsutomi1996 Mitsutomi, M., Ueda, M., Arai, M., Ando, A., Watanabe, T. (1996) Action patterns of microbial chitinases and chitosanases on partially ''N''-acetylated chitosan. Chitin Enzymology, vol. 2, pp 273-284.<br />
#Fukamizo1995 pmid=7487871<br />
#Boucher1995 pmid=8537367<br />
#Lacombe-Harvey2009 pmid=19143844<br />
#Saito1999 pmid=10521473<br />
#Marcotte1996 pmid=8564542<br />
#Fukamizo2005 pmid=16272568<br />
#Monzingo1996 pmid=8564539<br />
#Holm1994 pmid=8119396<br />
#Tremblay2001 pmid=11686931<br />
#Katsumi2005 pmid=16288718<br />
#Ando1992 Ando, A., Noguchi, K., Yanagi, M., Shinoyama, H., Kagawa, Y., Hirata, H., Yabuki, M., Fujii, T. (1992) Primary structure of chitosanase produced by ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 38:135-144.<br />
<br />
<br />
<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=3665Glycoside Hydrolase Family 462010-02-04T21:11:20Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 46 are essentially ''endo''-beta-1,4-chitosanases (EC 3.2.1.132) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits in chitosan, all the enzymes examined for their cleavage specificity recognized productively the GlcN-GlcN links. Furthermore, the chitosanase from ''Bacillus circulans'' MH-K1 recognized also GlcN-GlcNAc links <cite>Mitsutomi1996</cite>, while the chitosanase from ''Streptomyces'' sp. N174 recognized the GlcNAc-GlcN links <cite>Fukamizo1995</cite>. <br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes utilize an inverting mechanism, as shown by NMR <cite>Fukamizo1995</cite>.<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues have been identified by site-directed mutagenesis and crystallography in the chitosanase from Streptomyces sp. N174. The general acid residue is Glu22, while Asp40 is the general base residue <cite>Boucher1995 Marcotte1996</cite>. The latter could activate the nucleophilic water molecule with assistance from residue Thr45 <cite>Lacombe-Harvey2009</cite>. Analysis of sequence alignments as well as crystallographic evidence showed that the same function is played by residues Glu37, Asp55 and Thr60 in the chitosanase from ''Bacillus circulans'' MH-K1 <cite>Saito1999</cite>.<br />
<br />
<br />
== Three-dimensional structures ==<br />
Two structures have been solved using X-ray crystallography, for the chitosanases from Streptomyces sp. N174 <cite>Marcotte1996</cite> and from Bacillus circulans MH-K1 (wild-type enzyme <cite>Saito1999</cite> and mutant K218P <cite>Fukamizo2005</cite>. These enzymes have essentially an alpha-helical fold, with two globular domains separated by the active site cleft for substrate binding. The cleft is bordered on the upper face by a three-stranded beta-sheet. The structure is similar to the 3D fold of the well studied lysozyme of bacteriophage T4 of ''Escherichia coli'' belonging to family GH24 <cite>Marcotte1996</cite> and, to some extent, to the structures of lysozymes from families GH22, GH23 as well the chitinases from family GH19 <cite>Monzingo1996</cite>. These five families are sometimes grouped in the "lysozyme superfamily" <cite>Holm1994 Lacombe-Harvey2009</cite>. <br />
The crystal structures, completed by site-directed mutagenesis have also revealed several residues involved in substrate binding <cite>Marcotte1996 Fukamizo2005 Tremblay2001 Katsumi2005</cite>. While a 4+2 model of substrate binding has been initially proposed for a GlcN hexasaccharide <cite>Marcotte1996</cite>, the mode of binding was later established as being in conformity with a 3+3 model, based on the analysis of products of hydrolysis <cite>Tremblay2001</cite>. <br />
<br />
<br />
== Family Firsts ==<br />
;First primary sequence determination: Chitosanase from ''Bacillus circulans'' MH-K1 <cite>Ando1992</cite>.<br />
;First sterochemistry determination: Chitosanase from ''Streptomyces'' sp. N174 by NMR <cite>Fukamizo1995</cite>.<br />
;First catalytic nucleophile identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.<br />
;First general acid/base residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.<br />
;First 3-D structure: Chitosanase from ''Streptomyces'' sp. N174 by X-ray crystallography <cite>Marcotte1996</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.<br />
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, WA., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.<br />
#Mitsutomi1996 Mitsutomi, M., Ueda, M., Arai, M., Ando, A., Watanabe, T. (1996) Action patterns of microbial chitinases and chitosanases on partially ''N''-acetylated chitosan. Chitin Enzymology, vol. 2, pp 273-284.<br />
#Fukamizo1995 pmid=7487871<br />
#Boucher1995 pmid=8537367<br />
#Lacombe-Harvey2009 pmid=19143844<br />
#Saito1999 pmid=10521473<br />
#Marcotte1996 pmid=8564542<br />
#Fukamizo2005 pmid=16272568<br />
#Monzingo1996 pmid=8564539<br />
#Holm1994 pmid=8119396<br />
#Tremblay2001 pmid=11686931<br />
#Katsumi2005 pmid=16288718<br />
#Ando1992 Ando, A., Noguchi, K., Yanagi, M., Shinoyama, H., Kagawa, Y., Hirata, H., Yabuki, M., Fujii, T. (1992) Primary structure of chitosanase produced by ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 38:135-144.<br />
<br />
<br />
<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=3664Glycoside Hydrolase Family 462010-02-04T21:03:53Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 46 are essentially ''endo''-beta-1,4-chitosanases (EC 3.2.1.132) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits in chitosan, all the enzymes examined for their cleavage specificity recognized productively the GlcN-GlcN links. Furthermore, the chitosanase from ''Bacillus circulans'' MH-K1 recognized also GlcN-GlcNAc links <cite>Mitsutomi1996</cite>, while the chitosanase from ''Streptomyces'' sp. N174 recognized the GlcNAc-GlcN links <cite>Fukamizo1995</cite>. <br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes utilize an inverting mechanism, as shown by NMR <cite>Fukamizo1995</cite>.<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues have been identified by site-directed mutagenesis and crystallography in the chitosanase from Streptomyces sp. N174. The general acid residue is Glu22, while Asp40 is the general base residue <cite>Boucher1995 Marcotte1996</cite>. The latter could activate the nucleophilic water molecule with assistance from residue Thr45 <cite>Lacombe-Harvey2009</cite>. Analysis of sequence alignments as well as crystallographic evidence showed that the same function is played by residues Glu37, Asp55 and Thr60 in the chitosanase from ''Bacillus circulans'' MH-K1 <cite>Saito1999</cite>.<br />
<br />
<br />
== Three-dimensional structures ==<br />
Two structures have been solved using X-ray crystallography, for the chitosanases from Streptomyces sp. N174 <cite>Marcotte1996</cite> and from Bacillus circulans MH-K1 (wild-type enzyme <cite>Saito1999</cite> and mutant K218P <cite>Fukamizo2005</cite>. These enzymes have essentially an alpha-helical fold, with two globular domains separated by the active site cleft for substrate binding. The cleft is bordered on the upper face by a three-stranded beta-sheet. The structure is similar to the 3D fold of the well studied lysozyme of bacteriophage T4 of ''Escherichia coli'' belonging to family GH24 <cite>Marcotte1996</cite> and, to some extent, to the structures of lysozymes from families GH22, GH23 as well the chitinases from family GH19 <cite>Monzingo1996</cite>. These five families are sometimes grouped in the "lysozyme superfamily" <cite>Holm1994 Lacombe-Harvey2009</cite>. <br />
The crystal structures, completed by site-directed mutagenesis have also revealed several residues involved in substrate binding <cite>Marcotte1996 Fukamizo2005 Tremblay2001 Katsumi2005</cite>. While a 4+2 model of substrate binding has been initially proposed for a GlcN hexasaccharide <cite>Marcotte1996</cite>, the mode of binding was later established as being in conformity with a 3+3 model, based on the analysis of products of hydrolysis <cite>Tremblay2001</cite>. <br />
<br />
<br />
== Family Firsts ==<br />
;First sterochemistry determination: Chitosanase from ''Streptomyces'' sp. N174 by NMR <cite>Fukamizo1995</cite>.<br />
;First catalytic nucleophile identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.<br />
;First general acid/base residue identification: Chitosanase from ''Streptomyces'' sp. N174 by sequence conservation and mutagenesis <cite>Boucher1995</cite> and by X-ray crystallography <cite>Marcotte1996</cite>.<br />
;First 3-D structure: Chitosanase from ''Streptomyces'' sp. N174 by X-ray crystallography <cite>Marcotte1996</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.<br />
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, WA., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.<br />
#Mitsutomi1996 Mitsutomi, M., Ueda, M., Arai, M., Ando, A., Watanabe, T. (1996) Action patterns of microbial chitinases and chitosanases on partially ''N''-acetylated chitosan. Chitin Enzymology, vol. 2, pp 273-284.<br />
#Fukamizo1995 pmid=7487871<br />
#Boucher1995 pmid=8537367<br />
#Lacombe-Harvey2009 pmid=19143844<br />
#Saito1999 pmid=10521473<br />
#Marcotte1996 pmid=8564542<br />
#Fukamizo2005 pmid=16272568<br />
#Monzingo1996 pmid=8564539<br />
#Holm1994 pmid=8119396<br />
#Tremblay2001 pmid=11686931<br />
#Katsumi2005 pmid=16288718<br />
<br />
<br />
<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=3663Glycoside Hydrolase Family 462010-02-04T20:49:19Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 46 are essentially ''endo''-beta-1,4-chitosanases (EC 3.2.1.132) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits in chitosan, all the enzymes examined for their cleavage specificity recognized productively the GlcN-GlcN links. Furthermore, the chitosanase from ''Bacillus circulans'' MH-K1 recognized also GlcN-GlcNAc links <cite>Mitsutomi1996</cite>, while the chitosanase from ''Streptomyces'' sp. N174 recognized the GlcNAc-GlcN links <cite>Fukamizo1995</cite>. <br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes utilize an inverting mechanism, as shown by NMR <cite>Fukamizo1995</cite>.<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues have been identified by site-directed mutagenesis and crystallography in the chitosanase from Streptomyces sp. N174. The general acid residue is Glu22, while Asp40 is the general base residue <cite>Boucher1995 Marcotte1996</cite>. The latter could activate the nucleophilic water molecule with assistance from residue Thr45 <cite>Lacombe-Harvey2009</cite>. Analysis of sequence alignments as well as crystallographic evidence showed that the same function is played by residues Glu37, Asp55 and Thr60 in the chitosanase from Bacillus circulans MH-K1 <cite>Saito1999</cite>.<br />
<br />
<br />
== Three-dimensional structures ==<br />
Two structures have been solved using X-ray crystallography, for the chitosanases from Streptomyces sp. N174 <cite>Marcotte1996</cite> and from Bacillus circulans MH-K1 (wild-type enzyme <cite>Saito1999</cite> and mutant K218P <cite>Fukamizo2005</cite>. These enzymes have essentially an alpha-helical fold, with two globular domains separated by the active site cleft for substrate binding. The cleft is bordered on the upper face by a three-stranded beta-sheet. The structure is similar to the 3D fold of the well studied lysozyme of bacteriophage T4 of ''Escherichia coli'' belonging to family GH24 <cite>Marcotte1996</cite> and, to some extent, to the structures of lysozymes from families GH22, GH23 as well the chitinases from family GH19 <cite>Monzingo1996</cite>. The crystal structures, completed by site-directed mutagenesis have also revealed several residues involved in substrate binding <cite>Marcotte1996 Fukamizo2005 Tremblay2001 Katsumi2005</cite>. While a 4+2 model of substrate binding has been initially proposed for a GlcN hexasaccharide <Marcotte1996>, the mode of binding was later established as 3+3 based on the analysis of products of hydrolysis <cite>Tremblay2001</cite>. <br />
<br />
<br />
== Family Firsts ==<br />
;First sterochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
<br />
== References ==<br />
<biblio><br />
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.<br />
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, WA., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.<br />
#Mitsutomi1996 Mitsutomi, M., Ueda, M., Arai, M., Ando, A., Watanabe, T. (1996) Action patterns of microbial chitinases and chitosanases on partially ''N''-acetylated chitosan. Chitin Enzymology, vol. 2, pp 273-284.<br />
#Fukamizo1995 pmid=7487871<br />
#Boucher1995 pmid=8537367<br />
#Lacombe-Harvey2009 pmid=19143844<br />
#Saito1999 pmid=10521473<br />
#Marcotte1996 pmid=8564542<br />
#Fukamizo2005 pmid=16272568<br />
#Monzingo1996 pmid=8564539<br />
#Tremblay2001 pmid=11686931<br />
#Katsumi2005 pmid=16288718<br />
<br />
<br />
<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=3662Glycoside Hydrolase Family 462010-02-04T20:46:36Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 46 are essentially ''endo''-beta-1,4-chitosanases (EC 3.2.1.132) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits in chitosan, all the enzymes examined for their cleavage specificity recognized productively the GlcN-GlcN links. Furthermore, the chitosanase from ''Bacillus circulans'' MH-K1 recognized also GlcN-GlcNAc links <cite>Mitsutomi1996</cite>, while the chitosanase from ''Streptomyces'' sp. N174 recognized the GlcNAc-GlcN links <cite>Fukamizo1995</cite>. <br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes utilize an inverting mechanism, as shown by NMR <cite>Fukamizo1995</cite>.<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues have been identified by site-directed mutagenesis and crystallography in the chitosanase from Streptomyces sp. N174. The general acid residue is Glu22, while Asp40 is the general base residue <cite>Boucher1995 Marcotte1996</cite>. The latter could activate the nucleophilic water molecule with assistance from residue Thr45 <cite>Lacombe-Harvey2009</cite>. Analysis of sequence alignments as well as crystallographic evidence showed that the same function is played by residues Glu37, Asp55 and Thr60 in the chitosanase from Bacillus circulans MH-K1 <cite>Saito1999</cite>.<br />
<br />
<br />
== Three-dimensional structures ==<br />
Two structures have been solved using X-ray crystallography, for the chitosanases from Streptomyces sp. N174 <cite>Marcotte1996</cite> and from Bacillus circulans MH-K1 (wild-type enzyme <cite>Saito1999</cite> and mutant K218P <cite>Fukamizo2005</cite>. These enzymes have essentially an alpha-helical fold, with two globular domains separated by the active site cleft for substrate binding. The cleft is bordered on the upper face by a three-stranded beta-sheet. The structure is similar to the 3D fold of the well studied lysozyme of bacteriophage T4 of ''Escherichia coli'' belonging to family GH24 <cite>Marcotte1996</cite> and, to some extent, to the structures of lysozymes from families GH22, GH23 as well the chitinases from family GH19 <cite>Monzingo1996</cite>. The crystal structures, completed by site-directed mutagenesis have also revealed several residues involved in substrate binding <cite<Marcotte1996 Fukamizo2005 Tremblay2001 Katsumi2005</cite>. While a 4+2 model of substrate binding has been initially proposed for a GlcN hexasaccharide <Marcotte1996>, the mode of binding was later established as 3+3 based on the analysis of products of hydrolysis <cite>Tremblay2001</cite>. <br />
<br />
<br />
== Family Firsts ==<br />
;First sterochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
<br />
== References ==<br />
<biblio><br />
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.<br />
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, WA., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.<br />
#Mitsutomi1996 Mitsutomi, M., Ueda, M., Arai, M., Ando, A., Watanabe, T. (1996) Action patterns of microbial chitinases and chitosanases on partially ''N''-acetylated chitosan. Chitin Enzymology, vol. 2, pp 273-284.<br />
#Fukamizo1995 pmid=7487871<br />
#Boucher1995 pmid=8537367<br />
#Lacombe-Harvey2009 pmid=19143844<br />
#Saito1999 pmid=10521473<br />
#Marcotte1996 pmid=8564542<br />
#Fukamizo2005 pmid=16272568<br />
#Monzingo1996 pmid=8564539<br />
#Tremblay2001 pmid=11686931<br />
#Katsumi2005 pmid=16288718<br />
<br />
<br />
<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=3661Glycoside Hydrolase Family 462010-02-04T20:23:01Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 46 are essentially ''endo''-beta-1,4-chitosanases (EC 3.2.1.132) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits in chitosan, all the enzymes examined for their cleavage specificity recognized productively the GlcN-GlcN links. Furthermore, the chitosanase from ''Bacillus circulans'' MH-K1 recognized also GlcN-GlcNAc links <cite>Mitsutomi1996</cite>, while the chitosanase from ''Streptomyces'' sp. N174 recognized the GlcNAc-GlcN links <cite>Fukamizo1995</cite>. <br />
<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes utilize an inverting mechanism, as shown by NMR <cite>Fukamizo1995</cite>.<br />
<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues have been identified by site-directed mutagenesis and crystallography in the chitosanase from Streptomyces sp. N174. The general acid residue is Glu22, while Asp40 is the general base residue <cite>Boucher1995 Marcotte1996</cite>. The latter could activate the nucleophilic water molecule with assistance from residue Thr45 <cite>Lacombe-Harvey2009</cite>. Analysis of sequence alignments as well as crystallographic evidence showed that the same function is played by residues Glu37, Asp55 and Thr60 in the chitosanase from Bacillus circulans MH-K1 <cite>Saito1999</cite>.<br />
<br />
<br />
== Three-dimensional structures ==<br />
Two structures have been solved using X-ray crystallography, for the chitosanases from Streptomyces sp. N174 <cite>Marcotte1996</cite> and from Bacillus circulans MH-K1 (wild-type enzyme <cite>Saito1999</cite> and mutant K218P <cite>Fukamizo2005</cite>. These enzymes have essentially an alpha-helical fold, with two globular domains separated by the active site cleft for substrate binding. The cleft is bordered on the upper face by a three-stranded beta-sheet. The structure is similar to the 3D fold of the well studied lysozyme of bacteriophage T4 of ''Escherichia coli'' belonging to family GH24 <cite>Marcotte1996</cite> and, to some extent, to the structures of lysozymes from families GH22, GH23 as well the chitinases from family GH19 <cite>Monzingo1996</cite>. <br />
<br />
<br />
== Family Firsts ==<br />
;First sterochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
<br />
== References ==<br />
<biblio><br />
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.<br />
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, W. A., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.<br />
#Mitsutomi1996 Mitsutomi, M., Ueda, M., Arai, M., Ando, A., Watanabe, T. (1996) Action patterns of microbial chitinases and chitosanases on partially ''N''-acetylated chitosan. Chitin Enzymology, vol. 2, pp 273-284.<br />
#Fukamizo1995 pmid=7487871<br />
#Boucher1995 pmid=8537367<br />
#Lacombe-Harvey2009 pmid=19143844<br />
#Saito1999 pmid=10521473<br />
#Marcotte1996 pmid=8564542<br />
#Fukamizo2005 pmid=16272568<br />
#Monzingo1996 pmid=8564539<br />
<br />
<br />
<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=3660Glycoside Hydrolase Family 462010-02-04T19:56:40Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 46 are essentially ''endo''-beta-1,4-chitosanases (EC 3.2.1.132) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits in chitosan, all the enzymes examined for their cleavage specificity recognized productively the GlcN-GlcN links. Furthermore, the chitosanase from ''Bacillus circulans'' MH-K1 recognized also GlcN-GlcNAc links <cite>Mitsutomi1996</cite>, while the chitosanase from ''Streptomyces'' sp. N174 recognized the GlcNAc-GlcN links <cite>Fukamizo1995</cite>. <br />
<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes utilize an inverting mechanism, as shown by NMR <cite>Fukamizo1995</cite>.<br />
<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues have been identified by site-directed mutagenesis and crystallography in the chitosanase from Streptomyces sp. N174. The general acid residue is Glu22, while Asp40 is the general base residue <cite>Boucher1995 Marcotte1996</cite>. The latter could activate the nucleophilic water molecule with assistance from residue Thr45 <cite>Lacombe-Harvey2009</cite>. Analysis of sequence alignments as well as crystallographic evidence showed that the same function is played by residues Glu37, Asp55 and Thr60 in the chitosanase from Bacillus circulans MH-K1 <cite>Saito1999</cite>.<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 (citation).<br />
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
<br />
== References ==<br />
<biblio><br />
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.<br />
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, W. A., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.<br />
#Mitsutomi1996 Mitsutomi, M., Ueda, M., Arai, M., Ando, A., Watanabe, T. (1996) Action patterns of microbial chitinases and chitosanases on partially ''N''-acetylated chitosan. Chitin Enzymology, vol. 2, pp 273-284.<br />
#Fukamizo1995 pmid=7487871<br />
#Boucher1995 pmid=8537367<br />
#Lacombe-Harvey2009 pmid=19143844<br />
#Saito1999 pmid=10521473<br />
<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=3659Glycoside Hydrolase Family 462010-02-04T19:50:06Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 46 are essentially ''endo''-beta-1,4-chitosanases (EC 3.2.1.132) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits in chitosan, all the enzymes examined for their cleavage specificity recognized productively the GlcN-GlcN links. Furthermore, the chitosanase from ''Bacillus circulans'' MH-K1 recognized also GlcN-GlcNAc links <cite>Mitsutomi1996</cite>, while the chitosanase from ''Streptomyces'' sp. N174 recognized the GlcNAc-GlcN links <cite>Fukamizo1995</cite>. <br />
<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Family GH46 enzymes utilize an inverting mechanism, as shown by NMR <cite>Fukamizo1995</cite>.<br />
<br />
<br />
== Catalytic Residues ==<br />
The catalytic residues have been identified by site-directed mutagenesis and crystallography in the chitosanase from Streptomyces sp. N174. The general acid residue is Glu22, while Asp40 is the general base residue <cite>Boucher1995 Marcotte1996</cite>. The latter could activate the nucleophilic water molecule with assistance from residue Thr45 <cite>Lacombe-Harvey2009</cite>. <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 (citation).<br />
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
<br />
== References ==<br />
<biblio><br />
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.<br />
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, W. A., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.<br />
#Mitsutomi1996 Mitsutomi, M., Ueda, M., Arai, M., Ando, A., Watanabe, T. (1996) Action patterns of microbial chitinases and chitosanases on partially ''N''-acetylated chitosan. Chitin Enzymology, vol. 2, pp 273-284.<br />
#Fukamizo1995 pmid=7487871<br />
#Boucher1995 pmid=8537367<br />
#Lacombe-Harvey2009 pmid=19143844<br />
<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=3658Glycoside Hydrolase Family 462010-02-04T19:20:58Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 46 are essentially ''endo''-beta-1,4-chitosanases (EC 3.2.1.132) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits in chitosan, all the enzymes examined for their cleavage specificity recognized productively the GlcN-GlcN links. Furthermore, the chitosanase from ''Bacillus circulans'' MH-K1 recognized also GlcN-GlcNAc links <cite>Mitsutomi1996</cite>, while the chitosanase from ''Streptomyces'' sp. N174 recognized the GlcNAc-GlcN links <cite>Fukamizo1995</cite>. <br />
<br />
<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 (citation).<br />
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
<br />
== References ==<br />
<biblio><br />
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.<br />
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, W. A., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.<br />
#Mitsutomi1996 Mitsutomi, M., Ueda, M., Arai, M., Ando, A., Watanabe, T. (1996) Action patterns of microbial chitinases and chitosanases on partially ''N''-acetylated chitosan. Chitin Enzymology, vol. 2, pp 273-284.<br />
#Fukamizo1995 Fukamizo, T., Honda, Y., Goto, S., Boucher, I., Brzezinski, R. (1995) Reaction mechanism of chitosanase from ''Streptomyces'' sp. N174. Biochemical Journal 311:377-383. <br />
<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=3657Glycoside Hydrolase Family 462010-02-04T19:11:53Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 46 are essentially ''endo''-beta-1,4-chitosanases (EC 3.2.1.132) that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits, all the enzymes examined for their cleavage specificity recognized productively the GlcN-GlcN links. Furthermore, the chitosanase from ''Bacillus circulans'' MH-K1 recognizes also GlcN-GlcNAc links, while the chitosanase from ''Streptomyces'' sp. N174 recognizes the GlcNAc-GlcN links. <br />
<br />
<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 (citation).<br />
;First catalytic nucleophile identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation (citation).<br />
<br />
== References ==<br />
<biblio><br />
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270.<br />
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, W. A., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.<br />
<br />
<br />
</biblio><br />
<br />
[[Category:Glycoside Hydrolase Families|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=3656Glycoside Hydrolase Family 462010-02-04T19:08:46Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 46 are essentially ''endo''-beta-1,4-chitosanases (EC 3.2.1.132)that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc) <cite>Yabuki1988 Boucher1992</cite>. Among the four types of links occurring between these two kinds of subunits, all the enzymes examined for their cleavage specificity recognized productively the GlcN-GlcN links. Furthermore, the chitosanase from ''Bacillus circulans'' MH-K1 recognizes also GlcN-GlcNAc links, while the chitosanase from ''Streptomyces'' sp. N174 recognizes the GlcNAc-GlcN links. <br />
<br />
<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 />
#Yabuki1988 Yabuki, M., Uchiyama, A., Suzuki, K., Ando, A., Fujii, T. (1988) Purification and properties of chitosanase from ''Bacillus circulans'' MH-K1. Journal of General and Applied Microbiology 34:255-270<br />
#Boucher1992 Boucher, I., Dupuy, A., Vidal, P., Neugebauer, W. A., Brzezinski, R. (1992) Purification and characterization of a chitosanase from ''Streptomyces'' N174. Applied Microbiology and Biotechnology 38:188-193.<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|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=3655Glycoside Hydrolase Family 462010-02-04T18:53:53Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 46 are essentially ''endo''-beta-1,4-chitosanases (EC 3.2.1.132)that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc)<cite>1</cite>, <cite>2</cite>. Among the four types of links occurring between these two kinds of subunits, all the enzymes examined for their cleavage specificity recognized productively the GlcN-GlcN links. Furthermore, the chitosanase from ''Bacillus circulans'' MH-KI recognizes also GlcN-GlcNAc links, while the chitosanase from ''Streptomyces'' sp. N174 recognizes the GlcNAc-GlcN links. <br />
<br />
<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|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=3654Glycoside Hydrolase Family 462010-02-04T18:50:05Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Glycoside hydrolases of family 46 are essentially ''endo''-beta-1,4-chitosanases (EC 3.2.1.132)that hydrolyze various links in chitosan, a polymer of beta-1,4-linked D-glucosamine (GlcN) units with a variable content (mostly 0 - 35%) of N-acetyl-D-glucosamine (GlcNAc)<cite>1</cite>, <cite>2</cite>. Among the four types of links occurring between these two kinds of subunits, all the enzymes examined for their cleavage specificity recognized productively the GlcN-GlcN links. Furthermore, the chitosanase from ''Bacillus circulans'' MH-KI recognizes also GlcN-GlcNAc links, while the chitosanase from ''Streptomyces'' sp. N174 recognizes the GlcNAc-GlcN links. <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|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_46&diff=3653Glycoside Hydrolase Family 462010-02-04T18:28:19Z<p>Ryszard Brzezinski: </p>
<hr />
<div><!-- CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Ryszard Brzezinski^^^<br />
* [[Responsible Curator]]: ^^^Ryszard Brzezinski^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GHnn'''<br />
|-<br />
|'''Clan''' <br />
|GH-I<br />
|-<br />
|'''Mechanism'''<br />
|inverting<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/GH46.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><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|GH046]]</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=User:Ryszard_Brzezinski&diff=3648User:Ryszard Brzezinski2010-02-01T18:23:36Z<p>Ryszard Brzezinski: </p>
<hr />
<div>'''Ryszard Brzezinski''' Université de Sherbrooke, Faculté des Sciences, Département de Biologie; 2500 boul. de l'Université, Sherbrooke, Québec, J1K 2R1, Canada<br />
<br />
Professor at the U of Sherbrooke (from 1985)<br />
<br />
PhD with Prof. Andrzej Piekarowicz (Warsaw University, Poland) working on purification and characterization of type III DNA restriction endonucleases from ''Haemophilus influenzae'' 1977-1980<br />
<br />
MSc with Prof. <br />
Mirosława Włodarczyk (Warsaw Uniwersity, Poland) working on mechanisms of conjugation in ''Escherichia coli''.<br />
<br />
Research interests: glycoside hydrolases enzymology (mainly ''endo''- and ''exo''-chitosanases), molecular biology of actinomycetes, environmental microbiology<br />
<br />
<br />
CAZyme Protein structures I have contributed to:<br />
<br />
GH2 from ''Amycolatopsis orientalis''<br />
<br />
GH46 from ''Streptomyces'' sp. N174</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=User:Ryszard_Brzezinski&diff=3647User:Ryszard Brzezinski2010-02-01T18:22:17Z<p>Ryszard Brzezinski: </p>
<hr />
<div>'''From CAZypedia'''<br />
<br />
'''Ryszard Brzezinski''' Université de Sherbrooke, Faculté des Sciences, Département de Biologie; 2500 boul. de l'Université, Sherbrooke, Québec, J1K 2R1, Canada<br />
<br />
Professor at the U of Sherbrooke (from 1985)<br />
<br />
PhD with Prof. Andrzej Piekarowicz (Warsaw University, Poland) working on purification and characterization of type III DNA restriction endonucleases from ''Haemophilus influenzae'' 1977-1980<br />
<br />
MSc with Prof. <br />
Mirosława Włodarczyk (Warsaw Uniwersity, Poland) working on mechanisms of conjugation in ''Escherichia coli''.<br />
<br />
Research interests: glycoside hydrolases enzymology (mainly ''endo''- and ''exo''-chitosanases), molecular biology of actinomycetes, environmental microbiology<br />
<br />
<br />
CAZyme Protein structures I have contributed to:<br />
<br />
GH2 from ''Amycolatopsis orientalis''<br />
<br />
GH46 from ''Streptomyces'' sp. N174</div>Ryszard Brzezinskihttps://www.cazypedia.org/index.php?title=User:Ryszard_Brzezinski&diff=3646User:Ryszard Brzezinski2010-02-01T18:11:45Z<p>Ryszard Brzezinski: Created page with ''''From CAZypedia''' '''Ryszard Brzezinski''' Université de Sherbrooke, Faculté des Sciences, Département de Biologie; 2500 boul. de l'Université, Sherbrooke, Québec, J1K 2…'</p>
<hr />
<div>'''From CAZypedia'''<br />
<br />
'''Ryszard Brzezinski''' Université de Sherbrooke, Faculté des Sciences, Département de Biologie; 2500 boul. de l'Université, Sherbrooke, Québec, J1K 2R1, Canada<br />
<br />
Currently Professor at the U of Sherbrooke (from 1985)<br />
<br />
PhD with Prof. Andrzej Piekarowicz (Warsaw University, Poland) working on purification and characterization of type III DNA restriction endonucleases from ''Haemophilus influenzae'' 1977-1980<br />
<br />
MSc with Prof. <br />
Mirosława Włodarczyk (Warsaw Uniwersity, Poland) working on mechanisms of conjugation in ''Escherichia coli''.<br />
<br />
<br />
CAZyme Protein structures I have contributed to:<br />
<br />
GH2 from ''Amycolatopsis orientalis''<br />
<br />
GH46 from ''Streptomyces'' sp. N174</div>Ryszard Brzezinski