Carboxypeptidase T

Carboxypeptidase T
Identifiers
EC number	3.4.17.18
CAS number	89623-65-4
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

Carboxypeptidase T (EC 3.4.17.18, CPT) is an enzyme.^[1][2][3] This enzyme catalyses the following chemical reaction

Releases a C-terminal residue, which may be hydrophobic or positively charged

This enzyme is isolated from Thermoactinomyces vulgaris.

References

1. Osterman, A.L., Stepanov, V.M., Rudenskaya, G.N., Khodova, O.M., Tsaplina, I.A., Yakovleva, M.B. and Loginova, L.G. (1984). "Carboxypeptidase T - an extracellular carboxypeptidase of thermophilic actinomycetes - a remote analog of animal carboxypeptidases". Biochemistry (Moscow) 49: 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. (1991). "Molecular cloning and primary structure of Thermoactinomyces vulgaris carboxypeptidase T: a metalloenzyme endowed with dual substrate specificity". FEBS Lett. 291: 75–78. doi:10.1016/0014-5793(91)81107-j. 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. (1992). "Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris". Eur. J. Biochem. 208: 281–288. doi:10.1111/j.1432-1033.1992.tb17184.x. PMID 1521526.

External links

• Carboxypeptidase T at the US National Library of Medicine Medical Subject Headings (MeSH)