ExplorEnz: EC 3.2.1.132

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3.2.1.132

Accepted name:

chitosanase

Reaction:

Endohydrolysis of β-(1→4)-linkages between D-glucosamine residues in a partly acetylated chitosan

Systematic name:

chitosan N-acetylglucosaminohydrolase

Comments:

A whole spectrum of chitosanases are now known (for more details, see http://rbrzezinski.recherche.usherbrooke.ca/). 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:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 51570-20-8

References:

1.	Fenton, D.M. and Eveleigh, D.E. Purification and mode of action of a chitosanase from Penicillium islandicum. J. Gen. Microbiol. 126 (1981) 151–165.
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 (1999) 30818–30825. [DOI] [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 (1992) 448–453. [DOI] [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 (1996) 155–162. [PMID: 8564542]

[EC 3.2.1.132 created 1990, modified 2004]