| 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. [DOI] [PMID: 6768556] |
| 4. |
Polgár, L. Structure and function of serine proteases. In: Neuberger, A. and Brocklehurst, K. (Ed.), 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. [DOI] [PMID: 2917002] |
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| [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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