The Enzyme Database

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EC 3.4.17.16     
Accepted name: membrane Pro-Xaa carboxypeptidase
Reaction: Release of a C-terminal residue other than proline, by preferential cleavage of a prolyl bond
Other name(s): carboxypeptidase P; microsomal carboxypeptidase; membrane Pro-X carboxypeptidase
Comments: One of the renal brush border exopeptidases
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9075-64-3
References:
1.  Dehm, P. and Nordwig, A. The cleavage of prolyl peptides by kidney peptidases. Isolation of a microsomal carboxypeptidase from swine kidney. Eur. J. Biochem. 17 (1970) 372–377. [PMID: 5500406]
2.  Booth, A.G., Hubbard, L.M.L. and Kenny, A.J. Proteins of the kidney microvillar membrane. Immunoelectrophoretic analysis of the membrane hydrolase: identification and resolution of the detergent- and proteinase-solubilized forms. Biochem. J. 179 (1979) 397–405. [PMID: 486090]
3.  Hedeager-Sorensen, S. and Kenny, A.J. Proteins of the kidney microvillar membrane. Purification and properties of carboxypeptidase P from pig kidneys. Biochem. J. 229 (1985) 251–257. [PMID: 4038259]
[EC 3.4.17.16 created 1992]
 
 


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