| Membrane Pro-Xaa carboxypeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.17.16 | ||||||||
| CAS no. | 9075-64-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Membrane Pro-Xaa carboxypeptidase (EC 3.4.17.16, carboxypeptidase P, microsomal carboxypeptidase) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Release of a C-terminal residue other than proline, by preferential cleavage of a prolyl bond
This is one of the renal brush border exopeptidases
References[edit]
- ^ Dehm P, Nordwig A (December 1970). "The cleavage of prolyl peptides by kidney peptidases. Isolation of a microsomal carboxypeptidase from swine kidney". European Journal of Biochemistry. 17 (2): 372–7. doi:10.1111/j.1432-1033.1970.tb01175.x. PMID 5500406.
- ^ Booth AG, Hubbard LM, Kenny AJ (May 1979). "Proteins of the kidney microvillar membrane. Immunoelectrophoretic analysis of the membrane hydrolases: identification and resolution of the detergent- and proteinase-solubilized forms". The Biochemical Journal. 179 (2): 397–405. doi:10.1042/bj1790397. PMC 1186637. PMID 486090.
- ^ Hedeager-Sørensen S, Kenny AJ (July 1985). "Proteins of the kidney microvillar membrane. Purification and properties of carboxypeptidase P from pig kidneys". The Biochemical Journal. 229 (1): 251–7. doi:10.1042/bj2290251. PMC 1145174. PMID 4038259.
External links[edit]
- Membrane+Pro-Xaa+carboxypeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
