Lysine carboxypeptidase
| Lysine carboxypeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.17.3 | ||||||||
| CAS no. | 9013-89-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Lysine carboxypeptidase (EC 3.4.17.3, carboxypeptidase N, arginine carboxypeptidase, kininase I, anaphylatoxin inactivator, plasma carboxypeptidase B, creatine kinase conversion factor, bradykinase, kininase Ia, hippuryllysine hydrolase, bradykinin-decomposing enzyme, protaminase, CPase N, creatinine kinase convertase, peptidyl-L-lysine(-L-arginine) hydrolase, CPN) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Release of a C-terminal basic amino acid, preferentially lysine
This is a zinc enzyme found in plasma. It inactivates bradykinin and anaphylatoxins.
References
- ^ Plummer TH, Erdös EG (1981). "Human plasma carboxypeptidase N". Methods in Enzymology. 80 Pt C: 442–9. doi:10.1016/s0076-6879(81)80038-9. PMID 7341915.
- ^ Levin Y, Skidgel RA, Erdös EG (August 1982). "Isolation and characterization of the subunits of human plasma carboxypeptidase N (kininase i)". Proceedings of the National Academy of Sciences of the United States of America. 79 (15): 4618–22. doi:10.1073/pnas.79.15.4618. PMC 346726. PMID 6750606.
- ^ 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.
External links
- Lysine+carboxypeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)