| EC |
3.4.17.12 |
| Accepted name: |
carboxypeptidase M |
| Reaction: |
Cleavage of C-terminal arginine or lysine residues from polypeptides |
| Other name(s): |
CPM |
| Comments: |
A membrane-bound enzyme optimally active at neutral pH. In peptidase family M14 (carboxypeptidase A family) |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 120038-28-0 |
| References: |
| 1. |
Skidgel, R.A. Basic carboxypeptidases: Regulators of peptide hormone activity. Trends Pharmacol. Sci. 9 (1988) 303–304. [DOI] [PMID: 3074547] |
| 2. |
Deddish, P.A., Skidgel, R.A. and Erdös, E.G. Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low pH. Biochem. J. 261 (1989) 289–291. [PMID: 2775217] |
| 3. |
Skidgel, R.A., Davis, R.M. and Tan, F. Human carboxypeptidase M. Purification and characterization of membrane-bound carboxypeptidase that cleaves peptide hormones. J. Biol. Chem. 264 (1989) 2236–2241. [PMID: 2914904] |
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| [EC 3.4.17.12 created 1992] |
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