Membrane dipeptidase

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Membrane dipeptidase
Identifiers
EC number3.4.13.19
CAS number9031-99-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB 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[edit]

References[edit]

  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.

External links[edit]