Membrane dipeptidase

Membrane dipeptidase
EC number
CAS number 9031-99-6
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Membrane dipeptidase (EC, renal dipeptidase, dehydropeptidase I (DPH I), dipeptidase, aminodipeptidase, dipeptide hydrolase, dipeptidyl hydrolase, nonspecific dipeptidase, glycosyl-phosphatidylinositol-anchored renal dipeptidase, MBD, MDP, leukotriene D4 hydrolase) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction

Hydrolysis of dipeptides (e.g., leukotriene D4, cystinyl-bis-glycine, some β-lactam antibiotics (e.g., carbapenem))

This membrane-bound, zinc enzyme has broad specificity.

Inhibitors include bestatin and cilastatin.



  1. Campbell, B.; Lin, H.; Davis, R.; Ballew, E. (1966). "The purification and properties of a particulate renal dipeptidase". Biochim. Biophys. Acta. 118 (2): 371–386. doi:10.1016/s0926-6593(66)80046-2. PMID 5961612.
  2. Campbell, B.J. (1970). "Renal dipeptidase". Methods Enzymol. 19: 722–729. doi:10.1016/0076-6879(70)19059-8.
  3. Kropp, H.; Sundelof, J.G.; Hajdu, R.; Kahan, F.M. (1982). "Metabolism of thienamycin and related carbapenem antibiotics by renal dipeptidase, dehydropeptidase-I". Antimicrob. Agents Chemother. 22 (1): 62–70. doi:10.1128/aac.22.1.62. PMID 7125632.
  4. Hooper, N.M.; Keen, J.N.; Turner, A.J. (1990). "Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme". Biochem. J. 265 (2): 429–433. PMC 1136904Freely accessible. PMID 2137335.
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