EC 3.4.13.19 - Membrane dipeptidase

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IntEnz Enzyme Nomenclature
EC 3.4.13.19

Names

Accepted name:
membrane dipeptidase
Other names:
MDP
aminodipeptidase
dehydropeptidase I (DPH I)
dipeptidase [ambiguous]
dipeptide hydrolase [ambiguous]
dipeptidyl hydrolase [ambiguous]
glycosyl-phosphatidylinositol-anchored renal dipeptidase
nonspecific dipeptidase
renal dipeptidase
microsomal dipeptidase
dehydropeptidase I
DPH I
Systematic name:
-

Reaction

Cofactor

Comments:

A membrane-bound, zinc enzyme with broad specificity. Abundant in the kidney cortex. Inhibited by bestatin and cilastatin. Type example of peptidase family M19.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00678
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004237
CAS Registry Number: 9031-99-6
UniProtKB/Swiss-Prot: (32) [show] [UniProt]

References

  1. Campbell, B., Lin, H., Davis, R. and Ballew, E.
    The purification and properties of a particulate renal dipeptidase.
    Biochim. Biophys. Acta 118: 371-386 (1966). [PMID: 5961612]
  2. Campbell, B.J.
    Renal dipeptidase.
    Methods Enzymol. 19: 722-729 (1970).
  3. Kropp, H., Sundelof, J.G., Hajdu, R. and Kahan, F.M.
    Metabolism of thienamycin and related carbapenem antibiotics by renal dipeptidase, dehydropeptidase-I.
    Antimicrob. Agents Chemother. 22: 62-70 (1982). [PMID: 7125632]
  4. Hooper, N.M., Keen, J.N. and Turner, A.J.
    Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme.
    Biochem. J. 265: 429-433 (1990). [PMID: 2137335]

[EC 3.4.13.19 created 1961 as EC 3.4.3.1 and EC 3.4.3.2, transferred 1972 to EC 3.4.13.1 and EC 3.4.13.2, transferred 1978 to EC 3.4.13.11, part transferred 1992 to EC 3.4.13.19, modified 2011]