Carboxypeptidase T (EC 3.4.17.18, CPT) is a hydrolytic enzyme.[1][2][3] This enzyme catalyses the following chemical reaction:
| Carboxypeptidase T | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.17.18 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
- Releases a C-terminal residue, which may be hydrophobic or positively charged.
This enzyme is isolated from Thermoactinomyces vulgaris.
References
edit- ^ Osterman AL, Stepanov VM, Rudenskaia GN, Khodova OM, Tsaplina IA (February 1984). "[Carboxypeptidase T--intracellular carboxypeptidase of Thermoactinomycetes--a distant analog of animal carboxypeptidase]". Biokhimiia. 49 (2): 292–301. PMID 6424730.
- ^ Smulevitch SV, Osterman AL, Galperina OV, Matz MV, Zagnitko OP, Kadyrov RM, Tsaplina IA, Grishin NV, Chestukhina GG, Stepanov VM (October 1991). "Molecular cloning and primary structure of Thermoactinomyces vulgaris carboxypeptidase T. A metalloenzyme endowed with dual substrate specificity". FEBS Letters. 291 (1): 75–8. 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 (September 1992). "Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris". European Journal of Biochemistry. 208 (2): 281–8. doi:10.1111/j.1432-1033.1992.tb17184.x. PMID 1521526.
External links
edit- Carboxypeptidase+T at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
