Leukotriene-B4 20-monooxygenase

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In enzymology, a leukotriene-B4 20-monooxygenase (EC 1.14.13.30) is an enzyme that catalyzes the chemical reaction

(6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + NADPH + H⁺ + O₂ $\rightleftharpoons$ (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.

[edit] References

IUBMB entry for 1.14.13.30
BRENDA references for 1.14.13.30 (Recommended.)
PubMed references for 1.14.13.30
PubMed Central references for 1.14.13.30
Google Scholar references for 1.14.13.30
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: 1590–5. 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: 1218–28. doi:10.1172/JCI112077. 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: 2292–5. doi:10.1073/pnas.82.8.2292. PMID 2986111.