Carboxypeptidase M Explained
Carboxypeptidase M |
Ec Number: | 3.4.17.12 |
Cas Number: | 120038-28-0 |
Carboxypeptidase M (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.
Notes and References
- Skidgel RA . Basic carboxypeptidases: regulators of peptide hormone activity . Trends in Pharmacological Sciences . 9 . 8 . 299–304 . August 1988 . 3074547 . 10.1016/0165-6147(88)90015-6 .
- Deddish PA, Skidgel RA, Erdös EG . Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low pH. Similarity to carboxypeptidase H (enkephalin convertase) . The Biochemical Journal . 261 . 1 . 289–91 . July 1989 . 2775217 . 1138816 .
- Skidgel RA, Davis RM, Tan F . Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones . The Journal of Biological Chemistry . 264 . 4 . 2236–41 . February 1989 . 2914904 .