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Glycoside Hydrolase Family 80
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|Glycoside Hydrolase Family GH80|
|Active site residues||inferred|
|CAZy DB link|
Glycoside hydrolase family GH80 is comprised of endo-acting β-1,4-chitosanases of bacterial origin. The first characterized member was from a proteobacterium  belonging to the Bacteroidetes/Chlorobi group [2, 3]. At present (July 2011), GH80 is very small family, comprised of fewer than 20 members.
Characterized GH80 members do not hydrolyze chitin or cellulose [1, 3], and for one member, the chitosan hexa-oligosaccharide (GlcN)6 is preferentially hydrolyzed into two molecules of the trisaccharide .
Kinetics and Mechanism
The stereochemistry of the hydrolytic reaction catalyzed by GH80 members has not yet been studied. However, sequence similarity with members of Clan GH-I suggests that these enzymes may operate with inversion of the anomeric configuration (see Catalytic Residues, below)
A site-directed mutagenesis study of the chitosanase A from Matsuebacter chitosanotabidus 3001 (new name: Mitsuaria chitosanitabida ) identified two residues as essentiel for catalysis: Glu-121 (in the sequence YPENG)and Glu-141 (in the sequence DYEAA) .
- First primary sequence determination
- Chitosanase ChoA from Matsuebacter chitosanotabidus 3001 (now Mitsuaria chitosanitabida) [1, 8]
- 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
- Park JK, Shimono K, Ochiai N, Shigeru K, Kurita M, Ohta Y, Tanaka K, Matsuda H, and Kawamukai M. (1999). Purification, characterization, and gene analysis of a chitosanase (ChoA) from Matsuebacter chitosanotabidus 3001. J Bacteriol. 1999;181(21):6642-9. DOI:10.1128/JB.181.21.6642-6649.1999 |
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.
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.
- Shimono K, Shigeru K, Tsuchiya A, Itou N, Ohta Y, Tanaka K, Nakagawa T, Matsuda H, and Kawamukai M. (2002). Two glutamic acids in chitosanase A from Matsuebacter chitosanotabidus 3001 are the catalytically important residues. J Biochem. 2002;131(1):87-96. DOI:10.1093/oxfordjournals.jbchem.a003081 |
- Sigrist CJ, Cerutti L, de Castro E, Langendijk-Genevaux PS, Bulliard V, Bairoch A, and Hulo N. (2010). PROSITE, a protein domain database for functional characterization and annotation. Nucleic Acids Res. 2010;38(Database issue):D161-6. DOI:10.1093/nar/gkp885 |
- Tremblay H, Blanchard J, and Brzezinski R. (2000). A common molecular signature unifies the chitosanases belonging to families 46 and 80 of glycoside hydrolases. Can J Microbiol. 2000;46(10):952-5. | Google Books | Open Library
- Amakata D, Matsuo Y, Shimono K, Park JK, Yun CS, Matsuda H, Yokota A, and Kawamukai M. (2005). Mitsuaria chitosanitabida gen. nov., sp. nov., an aerobic, chitosanase-producing member of the 'Betaproteobacteria'. Int J Syst Evol Microbiol. 2005;55(Pt 5):1927-1932. DOI:10.1099/ijs.0.63629-0 |