From Wikipedia, the free encyclopedia
Chitosanase
Identifiers
EC no. 3.2.1.132
CAS no. 51570-20-8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Chitosanase ( EC 3.2.1.132) is an enzyme with systematic name chitosan N-acetylglucosaminohydrolase. [1] [2] [3] [4] This enzyme catalyses the following chemical reaction

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

A whole spectrum of chitosanases are known.

References

  1. ^ Fenton DM, Eveleigh DE (1981). "Purification and mode of action of a chitosanase from Penicillium islandicum". J. Gen. Microbiol. 126: 151–165. doi: 10.1099/00221287-126-1-151.
  2. ^ Saito J, Kita A, Higuchi Y, Nagata Y, Ando A, Miki K (October 1999). "Crystal structure of chitosanase from Bacillus circulans MH-K1 at 1.6-A resolution and its substrate recognition mechanism". The Journal of Biological Chemistry. 274 (43): 30818–25. doi: 10.1074/jbc.274.43.30818. PMID  10521473.
  3. ^ Izume M, Nagae S, Kawagishi H, Mitsutomi M, Ohtakara A (March 1992). "Action pattern of Bacillus sp. no. 7-M chitosanase on partially N-acetylated chitosan". Bioscience, Biotechnology, and Biochemistry. 56 (3): 448–53. doi: 10.1271/bbb.56.448. PMID  1368330.
  4. ^ Marcotte EM, Monzingo AF, Ernst SR, Brzezinski R, Robertus JD (February 1996). "X-ray structure of an anti-fungal chitosanase from streptomyces N174". Nature Structural Biology. 3 (2): 155–62. doi: 10.1038/nsb0296-155. PMID  8564542.
From Wikipedia, the free encyclopedia
Chitosanase
Identifiers
EC no. 3.2.1.132
CAS no. 51570-20-8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Chitosanase ( EC 3.2.1.132) is an enzyme with systematic name chitosan N-acetylglucosaminohydrolase. [1] [2] [3] [4] This enzyme catalyses the following chemical reaction

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

A whole spectrum of chitosanases are known.

References

  1. ^ Fenton DM, Eveleigh DE (1981). "Purification and mode of action of a chitosanase from Penicillium islandicum". J. Gen. Microbiol. 126: 151–165. doi: 10.1099/00221287-126-1-151.
  2. ^ Saito J, Kita A, Higuchi Y, Nagata Y, Ando A, Miki K (October 1999). "Crystal structure of chitosanase from Bacillus circulans MH-K1 at 1.6-A resolution and its substrate recognition mechanism". The Journal of Biological Chemistry. 274 (43): 30818–25. doi: 10.1074/jbc.274.43.30818. PMID  10521473.
  3. ^ Izume M, Nagae S, Kawagishi H, Mitsutomi M, Ohtakara A (March 1992). "Action pattern of Bacillus sp. no. 7-M chitosanase on partially N-acetylated chitosan". Bioscience, Biotechnology, and Biochemistry. 56 (3): 448–53. doi: 10.1271/bbb.56.448. PMID  1368330.
  4. ^ Marcotte EM, Monzingo AF, Ernst SR, Brzezinski R, Robertus JD (February 1996). "X-ray structure of an anti-fungal chitosanase from streptomyces N174". Nature Structural Biology. 3 (2): 155–62. doi: 10.1038/nsb0296-155. PMID  8564542.

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