EC 220.127.116.11 - Membrane dipeptidase
IntEnz Enzyme Nomenclature
dehydropeptidase I (DPH I)
dipeptide hydrolase [ambiguous]
dipeptidyl hydrolase [ambiguous]
glycosyl-phosphatidylinositol-anchored renal dipeptidase
48940 [IUBMB]an L-aminoacyl-L-amino acidan L-aminoacyl-L-amino acidName origin: UniProt - CHECKED (C)Formula: C4H6N2O3R2
Charge: 0ChEBI compound status: CHECKED (C)H2OH2OName origin: UniProt - CHECKED (C)Formula: H2O
Charge: 0ChEBI compound status: CHECKED (C)<?>2
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
The purification and properties of a particulate renal dipeptidase.Biochim. Biophys. Acta 118: 371-386 (1966). [PMID: 5961612]
Renal dipeptidase.Methods Enzymol. 19: 722-729 (1970).
Metabolism of thienamycin and related carbapenem antibiotics by renal dipeptidase, dehydropeptidase-I.Antimicrob. Agents Chemother. 22: 62-70 (1982). [PMID: 7125632]
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 18.104.22.168 created 1961 as EC 22.214.171.124 and EC 126.96.36.199, transferred 1972 to EC 188.8.131.52 and EC 184.108.40.206, transferred 1978 to EC 220.127.116.11, part transferred 1992 to EC 18.104.22.168, modified 2011]