Glycoside Hydrolase Family 80

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• Author:
• Responsible Curator: ^^^Ryszard Brzezinski^^^

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Glycoside Hydrolase Family GH80
Clan	GH-I
Mechanism	not determined
Active site residues	inferred
CAZy DB link
https://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>

1. Park1999 pmid=10542164
2. 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.
3. 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.
4. Shimono2002 pmid=11754739
5. Tremblay2000 pmid=11068683
6. Sigrist2010 pmid=19858104
7. Amakata2005 pmid=16166689