In enzymology, a leukotriene-B4 20-monooxygenase (EC 1.14.13.30) is an enzyme that catalyzes the chemical reaction
| leukotriene-B4 20-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.30 | ||||||||
| CAS no. | 90119-11-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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- (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + NADPH + H+ + O2 (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14- tetraenoate + NADP+ + H2O
The 4 substrates of this enzyme are (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate, NADPH, H+, and O2, whereas its 4 products are (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-, tetraenoate, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate,N ADPH:oxygen oxidoreductase (20-hydroxylating). Other names in common use include leukotriene-B4 20-hydroxylase, leucotriene-B4 omega-hydroxylase, LTB4 20-hydroxylase, and LTB4 omega-hydroxylase. This enzyme participates in arachidonic acid metabolism. It employs one cofactor, heme.
References edit
- Romano MC, Eckardt RD, Bender PE, Leonard TB, Straub KM, Newton JF (1987). "Biochemical characterization of hepatic microsomal leukotriene B4 hydroxylases". J. Biol. Chem. 262 (4): 1590–5. doi:10.1016/S0021-9258(19)75676-2. PMID 3027095.
- Shak S, Goldstein IM (1985). "Leukotriene B4 omega-hydroxylase in human polymorphonuclear leukocytes. Partial purification and identification as a cytochrome P-450". J. Clin. Invest. 76 (3): 1218–28. doi:10.1172/JCI112077. PMC 424026. PMID 4044832.
- Soberman RJ, Harper TW, Murphy RC, Austen KF (1985). "Identification and functional characterization of leukotriene B4 20-hydroxylase of human polymorphonuclear leukocytes". Proc. Natl. Acad. Sci. U.S.A. 82 (8): 2292–5. doi:10.1073/pnas.82.8.2292. PMC 397543. PMID 2986111.
