KEGG   ENZYME: 3.4.17.16Help
Entry
EC 3.4.17.16                Enzyme                                 

Name
membrane Pro-Xaa carboxypeptidase;
carboxypeptidase P;
microsomal carboxypeptidase;
membrane Pro-X carboxypeptidase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metallocarboxypeptidases
BRITE hierarchy
Reaction(IUBMB)
Release of a C-terminal residue other than proline, by preferential cleavage of a prolyl bond
Comment
One of the renal brush border exopeptidases
History
EC 3.4.17.16 created 1992
Reference
1  [PMID:5500406]
  Authors
Dehm P, Nordwig A.
  Title
The cleavage of prolyl peptides by kidney peptidases. Isolation of a microsomal carboxypeptidase from swine kidney.
  Journal
Eur J Biochem 17:372-7 (1970)
DOI:10.1111/j.1432-1033.1970.tb01175.x
Reference
2  [PMID:486090]
  Authors
Booth AG, Hubbard LM, Kenny AJ.
  Title
Proteins of the kidney microvillar membrane. Immunoelectrophoretic analysis of the membrane hydrolases: identification and resolution of the detergent- and proteinase-solubilized forms.
  Journal
Biochem J 179:397-405 (1979)
Reference
3  [PMID:4038259]
  Authors
Hedeager-Sorensen S, Kenny AJ.
  Title
Proteins of the kidney microvillar membrane. Purification and properties of carboxypeptidase P from pig kidneys.
  Journal
Biochem J 229:251-7 (1985)
Other DBs
ExplorEnz - The Enzyme Database: 3.4.17.16
IUBMB Enzyme Nomenclature: 3.4.17.16
ExPASy - ENZYME nomenclature database: 3.4.17.16
BRENDA, the Enzyme Database: 3.4.17.16
CAS: 9075-64-3

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