Biology:Carboxypeptidase T
From HandWiki
| Carboxypeptidase T | |||||||||
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| 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 | ||||||||
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Carboxypeptidase T (EC 3.4.17.18, CPT) is a hydrolytic 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
- ↑ "[Carboxypeptidase T--intracellular carboxypeptidase of Thermoactinomycetes--a distant analog of animal carboxypeptidase]". Biokhimiia 49 (2): 292–301. February 1984. PMID 6424730.
- ↑ "Molecular cloning and primary structure of Thermoactinomyces vulgaris carboxypeptidase T. A metalloenzyme endowed with dual substrate specificity". FEBS Letters 291 (1): 75–8. October 1991. doi:10.1016/0014-5793(91)81107-j. PMID 1936254.
- ↑ "Crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris". European Journal of Biochemistry 208 (2): 281–8. September 1992. 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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