Carboxypeptidase M
| Carboxypeptidase M | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.17.12 | ||||||||
| CAS no. | 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
[edit]- ^ Skidgel RA (August 1988). "Basic carboxypeptidases: regulators of peptide hormone activity". Trends in Pharmacological Sciences. 9 (8): 299–304. doi:10.1016/0165-6147(88)90015-6. PMID 3074547.
- ^ Deddish PA, Skidgel RA, Erdös EG (July 1989). "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. PMC 1138816. PMID 2775217.
- ^ Skidgel RA, Davis RM, Tan F (February 1989). "Human carboxypeptidase M. Purification and characterization of a membrane-bound carboxypeptidase that cleaves peptide hormones". The Journal of Biological Chemistry. 264 (4): 2236–41. PMID 2914904.
External links
[edit]- Carboxypeptidase+M at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
