Carboxypeptidase M

Carboxypeptidase M
Identifiers
EC number 3.4.17.12
CAS number 120038-28-0
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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

  1. 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.
  2. 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.
  3. 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.

External links

This article is issued from Wikipedia - version of the Tuesday, January 26, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.