EC 3.4.21.1 - Chymotrypsin

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IntEnz Enzyme Nomenclature
EC 3.4.21.1

Names

Accepted name:
chymotrypsin
Other names:
α-chymar
α-chymar ophth
α-chymotrypsin
α-chymotrypsin A
avazyme
chymar
chymotest
chymotrypsins A and B
enzeon
quimar
quimotrase
Systematic name:

Reaction

Comments:

Chymotrypsin A is formed from cattle and pig chymotrypsinogen A, several iso-forms being produced according to the number of bonds hydrolysed in the precursor. Formerly EC 3.4.4.5. Chymotrypsin B, formerly EC 3.4.4.6, formed from chymotrypsinogen B, is homologous with chymotrypsin A. Enzymes with specificity similar to that of chymotrypsins A and B have been isolated from many species. In peptidase family S1 (trypsin family).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , NIST 74 , UniPathway
Protein domains and families: PROSITE:PDOC00124
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004263
CAS Registry Number: 9004-07-3
UniProtKB/Swiss-Prot: (19) [show] [UniProt]

References

  1. Wilcox, P.E.
    Chymotrypsinogens - chymotrypsins.
    Methods Enzymol. 19: 64-108 (1970).
  2. Blow, D.M.
    Structure and mechanism of chymotrypsin.
    Acc. Chem. Res. 9: 145-152 (1976).
  3. Bauer, C.-A.
    Active centers of α-chymotrypsin and of Streptomyces griseus proteases 1 and 3.
    Eur. J. Biochem. 105: 565-570 (1980). [PMID: 6768556]
  4. Polgár, L.
    Structure and function of serine proteases.
    In: Neuberger, A. and Brocklehurst, K. (Eds.) Hydrolytic Enzymes. New Comprehensive Biochemistry vol. 16, Elsevier, Amsterdam, 1987, 159-200
  5. Tomita, N., Izumoto, Y., Horii, A., Doi, S., Yokouchi, H., Ogawa, M., Mori, T. and Matsubara, K.
    Molecular cloning and nucleotide sequence of human pancreatic prechymotrypsinogen cDNA.
    Biochem. Biophys. Res. Commun. 158: 569-575 (1989). [PMID: 2917002]

[EC 3.4.21.1 created 1961 as EC 3.4.4.5 and EC 3.4.4.6, transferred 1972 to EC 3.4.21.1]