|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 18.104.22.168
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.
Mass balance status: The left side is missing: R: 1 N: 1 C: 2 O: 1 H: 2
Enzyme Commission Primary Name: carboxypeptidase M
Enzyme Commission Synonyms: CPM
Taxonomic Range: Metazoa
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -48.12524 [Latendresse13]
Enzyme Commission Summary:
This enzyme catalyzes cleavage of C-terminal arginine or lysine residues from polypeptides.
A membrane-bound enzyme optimally active at neutral pH. In peptidase family M14 (carboxypeptidase A family).
Deddish89: Deddish PA, Skidgel RA, Erdos EG (1989). "Enhanced Co2+ activation and inhibitor binding of carboxypeptidase M at low pH. Similarity to carboxypeptidase H (enkephalin convertase)." Biochem J 261(1);289-91. PMID: 2775217
Skidgel89: Skidgel RA, Davis RM, Tan F (1989). "Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones." J Biol Chem 264(4);2236-41. PMID: 2914904
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