Membrane dipeptidase
(Redirected from Leukotriene D4 hydrolase)
| Membrane dipeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.13.19 | ||||||||
| CAS no. | 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
[edit]- Dipeptidase 1 (DPEP1)
- Dipeptidase 2 (DPEP2)
- Dipeptidase 3 (DPEP3)
References
[edit]- ^ Campbell BJ, Lin YC, Davis RV, Ballew E (May 1966). "The purification and properties of a particulate renal dipeptidase". Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation. 118 (2): 371–86. doi:10.1016/s0926-6593(66)80046-2. PMID 5961612.
- ^ Campbell, B.J. (1970). Renal dipeptidase. Methods Enzymol. Vol. 19. pp. 722–729. doi:10.1016/0076-6879(70)19059-8. ISBN 978-0-12-181881-4.
- ^ 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.
- ^ 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]- Membrane+dipeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
