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 BJ, Lin YC, Davis RV, Ballew E (May 1966). "The purification and properties of a particulate renal dipeptidase". Biochimica et Biophysica Acta. 118 (2): 371–86. 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 JG, Hajdu R, Kahan FM (July 1982). "Metabolism of thienamycin and related carbapenem antibiotics by the renal dipeptidase, dehydropeptidase". Antimicrobial Agents and Chemotherapy. 22 (1): 62–70. doi:10.1128/aac.22.1.62. PMC 183675. PMID 7125632.
  4. ↑ Hooper NM, Keen JN, Turner AJ (January 1990). "Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme". The Biochemical Journal. 265 (2): 429–33. doi:10.1042/bj2650429. PMC 1136904. PMID 2137335.
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