Monooxygenase
From Wikipedia, the free encyclopedia
| Monooxygenase | |||||||
|---|---|---|---|---|---|---|---|
 Structure of the TetX monooxygenase in complex with the substrate 7-Iodtetracycline.[1] | |||||||
| Identifiers | |||||||
| Symbol | FAD_binding_3 | ||||||
| Pfam | PF01494 | ||||||
| InterPro | IPR002938 | ||||||
| SCOP2 | 2phh / SCOPe / SUPFAM | ||||||
| |||||||
Monooxygenases are enzymes that incorporate one hydroxyl group (−OH) into substrates in many metabolic pathways. In this reaction, the two atoms of dioxygen are reduced to one hydroxyl group and one H2O molecule by the concomitant oxidation of NAD(P)H.[2][3] One important subset of the monooxygenases, the cytochrome P450 omega hydroxylases, is used by cells to metabolize arachidonic acid (i.e. eicosatetraenoic acid) to the cell signaling molecules, 20-hydroxyeicosatetraenoic acid or to reduce or totally inactivate the activate signaling molecules for example by hydroxylating leukotriene B4 to 20-hydroxy-leukotriene B5, 5-hydroxyeicosatetraenoic acid to 5,20-dihydroxyeicosatetraenoic acid, 5-oxo-eicosatetraenoic acid to 5-oxo-20-hydroxyeicosatetraenoic acid, 12-hydroxyeicosatetraenoic acid to 12,20-dihydroxyeicosatetraenoic acid, and epoxyeicosatrienoic acids to 20-hydroxy-epoxyeicosatrienoic acids.
They are classified as oxidoreductase enzymes that catalyze an electron transfer.
