The Enzyme Database

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EC 3.4.21.1     
Accepted name: chymotrypsin
Reaction: Preferential cleavage: Tyr┼, Trp┼, Phe┼, Leu┼
Other name(s): chymotrypsins A and B; α-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; α-chymar; α-chymotrypsin A; α-chymotrypsin
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. Chymotrypsin B (formerly listed as 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: BRENDA, EXPASY, GTD, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9004-07-3
References:
1.  Wilcox, P.E. Chymotrypsinogens - chymotrypsins. Methods Enzymol. 19 (1970) 64–108.
2.  Blow, D.M. Structure and mechanism of chymotrypsin. Acc. Chem. Res. 9 (1976) 145–152.
3.  Bauer, C.-A. Active centers of α-chymotrypsin and of Streptomyces griseus proteases 1 and 3. Eur. J. Biochem. 105 (1980) 565–570. [PMID: 6768556]
4.  Polgár, L. Structure and function of serine proteases. In: Neuberger, A. and Brocklehurst, K. (Eds), New Comprehensive Biochemistry: Hydrolytic Enzymes, vol. 16, Elsevier, Amsterdam, 1987, pp. 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 (1989) 569–575. [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]
 
 


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