The Enzyme Database

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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, 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]
[EC 3.4.17.12 created 1992]
 
 


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