Carboxypeptidase M
| Carboxypeptidase M | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.17.12 | ||||||||
| CAS no. | 120038-28-0 | ||||||||
| 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 M (EC 3.4.17.12, CPM) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Cleavage of C-terminal arginine or lysine residues from polypeptides
This is a membrane-bound enzyme optimally active at neutral pH.
References
- ^ Skidgel, R.A. (1988). "Basic carboxypeptidases: Regulators of peptide hormone activity". Trends Pharmacol. Sci. 9: 303–304. doi:10.1016/0165-6147(88)90015-6. PMID 3074547.
- ^ Deddish, P.A.; Skidgel, R.A.; Erdös, E.G. (1989). "Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low pH". Biochem. J. 261: 289–291. PMC 1138816. PMID 2775217.
- ^ Skidgel, R.A.; Davis, R.M.; Tan, F. (1989). "Human carboxypeptidase M. Purification and characterization of membrane-bound carboxypeptidase that cleaves peptide hormones". J. Biol. Chem. 264: 2236–2241. PMID 2914904.
External links
- Carboxypeptidase+M at the U.S. National Library of Medicine Medical Subject Headings (MeSH)