The Enzyme Database

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EC 3.4.17.18     
Accepted name: carboxypeptidase T
Reaction: Releases a C-terminal residue, which may be hydrophobic or positively charged
Other name(s): CPT (ambiguous)
Comments: Known from Thermoactinomyces vulgaris. In peptidase family M14 (carboxypeptidase A family)
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 89623-65-4
References:
1.  Osterman, A.L., Stepanov, V.M., Rudenskaya, G.N., Khodova, O.M., Tsaplina, I.A., Yakovleva, M.B. and Loginova, L.G. Carboxypeptidase T - an extracellular carboxypeptidase of thermophilic actinomycetes - a remote analog of animal carboxypeptidases. Biochemistry (USSR) 49 (1984) 292–301. [PMID: 6424730]
2.  Smulevitch, S.V., Osterman, A.L., Galperina, O.V., Matz, M.V., Zagnitko, O.P., Kadyrov, R.M., Tsaplina, I.A., Grishin, N.V., Chestukhina, G.G. and Stepanov, V.M. Molecular cloning and primary structure of Thermoactinomyces vulgaris carboxypeptidase T: a metalloenzyme endowed with dual substrate specificity. FEBS Lett. 291 (1991) 75–78. [DOI] [PMID: 1936254]
3.  Teplyakov, A., Polyakov, K., Obmolova, G., Strokopytov, B., Kuranova, I., Osterman, A., Grishin, N., Smulevitch, S., Zagnitko, O., Galperina, O., Matz, M. and Stepanov, V. Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris. Eur. J. Biochem. 208 (1992) 281–288. [DOI] [PMID: 1521526]
[EC 3.4.17.18 created 1993]
 
 


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