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, MDP) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction

Hydrolysis of dipeptides

This membrane-bound, zinc enzyme has broad specificity.

References

  1. ↑ Campbell, B., Lin, H., Davis, R. and 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. and 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. and 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 1136904. PMID 2137335.

External links