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MetaCyc Reaction: 3.4.17.12

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 3.4.17.12

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, 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 Inferred by computational analysis [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).

Citations: [Skidgel88, Deddish89, Skidgel89]

Relationship Links: BRENDA:EC:3.4.17.12 , ENZYME:EC:3.4.17.12 , IUBMB-ExplorEnz:EC:3.4.17.12


References

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

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Skidgel88: Skidgel RA (1988). "Basic carboxypeptidases: regulators of peptide hormone activity." Trends Pharmacol Sci 9(8);299-304. PMID: 3074547

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Sun Aug 30, 2015, BIOCYC14B.