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 | ||||||||
| |||||||||
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
- ↑ Osterman, A.L.; Stepanov, V.M.; Rudenskaya, G.N.; Khodova, O.M.; Tsaplina, I.A.; Yakovleva, M.B.; 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.
- ↑ 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.; 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.
- ↑ Teplyakov, A.; Polyakov, K.; Obmolova, G.; Strokopytov, B.; Kuranova, I.; Osterman, A.; Grishin, N.; Smulevitch, S.; Zagnitko, O.; Galperina, O.; Matz, M.; 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)
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