EC 3.2.1.132 - Chitosanase

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IntEnz Enzyme Nomenclature
EC 3.2.1.132

Names

Accepted name:
chitosanase
Systematic name:
chitosan N-acetylglucosaminohydrolase

Reaction

Comments:

A whole spectrum of chitosanases are now known (for more details, see http://pages.usherbrooke.ca/rbrzezinski/). They can hydrolyse various types of links in chitosan. The only constant property is the endohydrolysis of GlcN-GlcN links, which is common to all known chitosanases. One known chitosanase is limited to this link recognition [4], while the majority can also recognize GlcN-GlcNAc links or GlcNAc-GlcN links but not both. They also do not recognize GlcNAc-GlcNAc links in partly acetylated chitosan.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC60000
Structural data: CSA , EC2PDB
Gene Ontology: GO:0016977
UniProtKB/Swiss-Prot: (14) [show] [UniProt]

References

  1. Fenton, D.M. and Eveleigh, D.E.
    Purification and mode of action of a chitosanase from Penicillium islandicum.
    J. Gen. Microbiol. 126: 151-165 (1981).
  2. Saito, J.-I., Kita, A., Higuchi, Y., Nagata, Y., Ando, A. and Miki, K.
    Crystal structure of chitosanase from Bacillus circulans MH-K1 at 1.6-Å resolution and its substrate recognition mechanism.
    J. Biol. Chem. 274: 30818-30825 (1999). [PMID: 10521473]
  3. Izume, M., Nagae, S., Kawagishi, H., Mitsutomi, M. and Ohtakara, A.
    Action pattern of Bacillus sp. No. 7-M chitosanase on partially N-acetylated chitosan.
    Biosci. Biotechnol. Biochem. 56: 448-453 (1992). [PMID: 1368330]
  4. Marcotte, E.M., Monzingo, A.F., Ernst, S.R., Brzezinski, R. and Robertus, J.D.
    X-ray structure of an anti-fungal chitosanase from Streptomyces N174.
    Nat. Struct. Biol. 3: 155-162 (1996). [PMID: 8564542]

[EC 3.2.1.132 created 1990, modified 2004]