Carboxypeptidase M
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. and Erdös, E.G. (1989). "Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low pH". Biochem. J. 261: 289–291. PMID 2775217.
- ↑ Skidgel, R.A., Davis, R.M. and 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.
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