Biochemical properties of cytochrome P-450 in relation to steroid oxygenation.
The P-450 cytochromes have been characterized biochemically in recent years as a family of monooxygenases that reductively activate molecular oxygen for insertion into steroids and other physiologically occurring lipids. Many of these enzymes are also known to bind and oxygenate a host of foreign compounds, including alcohol, drugs, pesticides, anesthetics, and mutagens. Some of the poorly understood variations in congenital adrenal hyperplasia may represent nutritional effects on the P-450 oxygenase systems or the ability of xenobiotics to interfere with normal steroid metabolism by these versatile cytochromes.
D000312:Adrenal Hyperplasia, Congenital; D000818:Animals; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D006900:Hydroxylation; D007527:Isoenzymes / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D010100:Oxygen / Q000378:metabolism*; D013250:Steroid Hydroxylases / Q000172:deficiency*
D007527:Isoenzymes; D009249:NADP; D003577:Cytochrome P-450 Enzyme System; D013250:Steroid Hydroxylases; D010100:Oxygen