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Difference between revisions of "Glycoside Hydrolase Family 80"
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== Substrate specificities == | == Substrate specificities == | ||
Glycoside hydrolases of family 80 include bacterial proteins. They were characterized from proteobacteria <cite>Park1999</cite> of from species belonging to the Bacteroidetes/Chlorobi group <cite>Matsuda2001 Yi2004</cite>. They are beta-1,4-chitosanases with endo-splitting activity. Chitin or cellulose are not hydrolyzed <cite>Park1999 Yi2004</cite>. Chitosan hexamer (GlcN)<sub>6</sub> is preferentially hydrolyzed into two trimeric molecules <cite>Shimono2002</cite>. | 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>. | ||
| − | + | The chitosanases from family GH80 share a PROSITE signature motif with the chitosanases from family GH46 <cite>Tremblay2000 Sigrist2010</cite>. | |
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | + | No detailed studies available yet. | |
== Catalytic Residues == | == Catalytic Residues == | ||
| − | + | A site-directed mutagenesis study of the chitosanase A from Matsuebacter chitosanotabidus 3001 (new name: Mitsuaria chitosanitabida <cite>Amakata2005</cite>) identified two residues as essentiel for catalysis: Glu-121 (in the sequence YP<u>E</u>NG)and Glu-141 (in the sequence DY<u>E</u>AA) <cite>Shimono2002</cite>. | |
== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | + | No three-dimensional structure has been solved for this family. | |
== Family Firsts == | == Family Firsts == | ||
;First primary sequence determination: Chitosanase ChoA from Matsuebacter chitosanotabidus 3001 (now Mitsuaria chitosanitabida) <cite>Park1999 Amakata2005</cite> | ;First primary sequence determination: Chitosanase ChoA from Matsuebacter chitosanotabidus 3001 (now Mitsuaria chitosanitabida) <cite>Park1999 Amakata2005</cite> | ||
| − | ;First stereochemistry determination: | + | ;First stereochemistry determination: Not yet determined |
| − | ;First catalytic nucleophile identification: | + | ;First catalytic nucleophile identification: Not yet identified |
| − | ;First general acid/base residue identification: | + | ;First general acid/base residue identification: Not yet identified |
| − | ;First 3-D structure: | + | ;First 3-D structure: Not yet determined |
== References == | == References == | ||
Revision as of 09:52, 14 July 2011
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
- Author:
- Responsible Curator: ^^^Ryszard Brzezinski^^^
| Glycoside Hydrolase Family GH80 | |
| Clan | GH-I |
| Mechanism | not determined |
| Active site residues | inferred |
| CAZy DB link | |
| http://www.cazy.org/GH80.html | |
Substrate specificities
Glycoside hydrolases of family 80 include bacterial proteins. They were characterized from proteobacteria [1] of from species belonging to the Bacteroidetes/Chlorobi group [2, 3]. They are beta-1,4-chitosanases with endo-splitting activity. Chitin or cellulose are not hydrolyzed [1, 3]. Chitosan hexamer (GlcN)6 is preferentially hydrolyzed into two trimeric molecules [4]. The chitosanases from family GH80 share a PROSITE signature motif with the chitosanases from family GH46 [5, 6].
Kinetics and Mechanism
No detailed studies available yet.
Catalytic Residues
A site-directed mutagenesis study of the chitosanase A from Matsuebacter chitosanotabidus 3001 (new name: Mitsuaria chitosanitabida [7]) identified two residues as essentiel for catalysis: Glu-121 (in the sequence YPENG)and Glu-141 (in the sequence DYEAA) [4].
Three-dimensional structures
No three-dimensional structure has been solved for this family.
Family Firsts
- First primary sequence determination
- Chitosanase ChoA from Matsuebacter chitosanotabidus 3001 (now Mitsuaria chitosanitabida) [1, 7]
- First stereochemistry determination
- Not yet determined
- First catalytic nucleophile identification
- Not yet identified
- First general acid/base residue identification
- Not yet identified
- First 3-D structure
- Not yet determined
References
<biblio>
- Park1999 pmid=10542164
- Matsuda2001 Matsuda, Y., Iida, I., Shinogi, T., Kakutani, K., Nonomura, T., Toyoda, H. (2001) In vitro suppression of mycelial growth of Fusarium oxysporum by extracellular chitosanase of Sphingobacterium multivorum and cloning of the chitosanase gene csnSM1. J. Gen. Plant Pathol. 67, 318-324.
- Yi2004 Yi, J.-H., Jang, H.-K., Lee, S.-J., Lee, K.-E., Choi, S.-G. (2004) Purification and properties of chitosanase from chitinolytic beta-Proteobacterium KNU3. J. Microbiol. Biotechnol. 14, 337-343.
- Shimono2002 pmid=11754739
- Tremblay2000 pmid=11068683
- Sigrist2010 pmid=19858104
- Amakata2005 pmid=16166689