Lysine carboxypeptidase
| Lysine carboxypeptidase | |||||||||
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| Identifiers | |||||||||
| EC number | 3.4.17.3 | ||||||||
| CAS number | 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 | ||||||||
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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, T.H., Jr. and Erdös, E.G. (1981). "Human plasma carboxypeptidase N". Methods Enzymol. 80: 442–449. doi:10.1016/s0076-6879(81)80038-9. PMID 7341915.
- ↑ Levin, Y., Skidgel, R.A. and Erdös, E.G. (1982). "Isolation and characterization of the subunits of human plasma carboxypeptidase N (kininase I)". Proc. Natl. Acad. Sci. USA 79: 4618–4622. doi:10.1073/pnas.79.15.4618. PMID 6750606.
- ↑ Skidgel, R.A. (1988). "Basic carboxypeptidases: regulators of peptide hormone activity". Trends Pharmacol. Sci. 9: 301–303. doi:10.1016/0165-6147(88)90015-6. PMID 3074547.
External links
- Lysine carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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