Omega oxygenases: nonheme-iron enzymes and P450 cytochromes.
Enzymes that effect with ease one of the most difficult chemical reactions, hydroxylation of an unfunctionalized alkyl group, are of particular interest because highly reactive intermediates must be produced. A typical example, the hydroxylation of fatty acids in the omega position, is now known to occur widely in nature. The catalysts, which can be called "omega-oxygenases," also insert molecular oxygen into a variety of other substrates at positions removed from activating functional groups, as in steroids, eicosanoids, and numerous drugs and other xenobiotics. Progress in the characterization of bacterial nonheme-iron enzymes, and plant, bacterial, and mammalian P450 cytochromes that catalyze fatty acid omega-oxidation, and evidence for multiple functional oxidants are summarized.
Coon
Minor J
MJ
Department of Biological Chemistry, Medical School, University of Michigan, Ann Arbor, MI 48109, USA. mjcoon@umich.edu
D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D002384:Catalysis; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000378:metabolism* / Q000502:physiology; D019159:Nonheme Iron Proteins / Q000737:chemistry* / Q000378:metabolism* / Q000502:physiology; D010084:Oxidation-Reduction; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology
D001426:Bacterial Proteins; D019159:Nonheme Iron Proteins; D010940:Plant Proteins; D003577:Cytochrome P-450 Enzyme System