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Glycoside Hydrolase Family 80

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

Substrate specificities

Glycoside hydrolase family GH80 is comprised of endo-acting β-1,4-chitosanases of bacterial origin. The first characterized member was from a proteobacterium [1] 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 [4].

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)

Catalytic Residues

The chitosanases from family GH80 share a PROSITE signature motif [5] with the chitosanases from family GH46 [6]. Together with GH24, these three families comprise clan GH-I [7].

A site-directed mutagenesis study of the chitosanase A from Matsuebacter chitosanotabidus 3001 (new name: Mitsuaria chitosanitabida [8]) 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 yet been solved for this family. As a member of clan GH-I, a lysozyme-like α-β fold is suggested, based on known GH24 and GH46 structures.

Family Firsts

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


  1. Park JK, Shimono K, Ochiai N, Shigeru K, Kurita M, Ohta Y, Tanaka K, Matsuda H, and Kawamukai M. Purification, characterization, and gene analysis of a chitosanase (ChoA) from Matsuebacter chitosanotabidus 3001. J Bacteriol. 1999 Nov;181(21):6642-9. PubMed ID:10542164 | HubMed [Park1999]
  2. 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. [Matsuda2001]
  3. Yi, J.-H., Jang, H.-K., Lee, S.-J., Lee, K.-E., Choi, S.-G. (2004) Purification and properties of chitosanase from chitinolytic beta-Proteobacterium KNU3. J. Microbiol. Biotechnol. 14, 337-343. [Yi2004]
  4. Shimono K, Shigeru K, Tsuchiya A, Itou N, Ohta Y, Tanaka K, Nakagawa T, Matsuda H, and Kawamukai M. Two glutamic acids in chitosanase A from Matsuebacter chitosanotabidus 3001 are the catalytically important residues. J Biochem. 2002 Jan;131(1):87-96. PubMed ID:11754739 | HubMed [Shimono2002]
  5. Sigrist CJ, Cerutti L, de Castro E, Langendijk-Genevaux PS, Bulliard V, Bairoch A, and Hulo N. PROSITE, a protein domain database for functional characterization and annotation. Nucleic Acids Res. 2010 Jan;38(Database issue):D161-6. DOI:10.1093/nar/gkp885 | PubMed ID:19858104 | HubMed [Sigrist2010]
  6. Tremblay H, Blanchard J, and Brzezinski R. A common molecular signature unifies the chitosanases belonging to families 46 and 80 of glycoside hydrolases. Can J Microbiol. 2000 Oct;46(10):952-5. PubMed ID:11068683 | HubMed [Tremblay2000]
  7. [CAZYGHpage]
  8. Amakata D, Matsuo Y, Shimono K, Park JK, Yun CS, Matsuda H, Yokota A, and Kawamukai M. Mitsuaria chitosanitabida gen. nov., sp. nov., an aerobic, chitosanase-producing member of the 'Betaproteobacteria'. Int J Syst Evol Microbiol. 2005 Sep;55(Pt 5):1927-32. DOI:10.1099/ijs.0.63629-0 | PubMed ID:16166689 | HubMed [Amakata2005]
All Medline abstracts: PubMed | HubMed
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