Membrane dipeptidase explained
| Membrane dipeptidase |
| Ec Number: | 3.4.13.19 |
| Cas Number: | 9031-99-6 |
Membrane dipeptidase (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
Notes and References
- Campbell BJ, Lin YC, Davis RV, Ballew E . The purification and properties of a particulate renal dipeptidase . Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation . 118 . 2 . 371–86 . May 1966 . 5961612 . 10.1016/s0926-6593(66)80046-2 .
- Book: Renal dipeptidase . Campbell, B.J. . Methods Enzymol. . 1970 . 19 . 722–729 . 10.1016/0076-6879(70)19059-8. 978-0-12-181881-4 .
- Kropp H, Sundelof JG, Hajdu R, Kahan FM . Metabolism of thienamycin and related carbapenem antibiotics by the renal dipeptidase, dehydropeptidase . Antimicrobial Agents and Chemotherapy . 22 . 1 . 62–70 . July 1982 . 7125632 . 183675 . 10.1128/aac.22.1.62 .
- Hooper NM, Keen JN, Turner AJ . 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 . January 1990 . 2137335 . 1136904 . 10.1042/bj2650429 .
