Membrane dipeptidase

Membrane dipeptidase
Identifiers
EC number 3.4.13.19
CAS number 9031-99-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Membrane dipeptidase (EC 3.4.13.19, 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.

Genes

References

  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. PMID 5961612. doi:10.1016/s0926-6593(66)80046-2.
  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. PMC 183675Freely accessible. PMID 7125632. doi:10.1128/aac.22.1.62.
  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. doi:10.1042/bj2650429.
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