Isolation, structural organization and mechanism of action of mitochondrial steroid hydroxylating systems.
A scheme for the isolation of individual proteins of the 20S,22R-cholesterol hydroxylating system is presented. Physico-chemical and structural parameters of cytochrome P-450 are furnished. Self-reconstitution of indivudal proteins of the system into an enzyme unit is shown. Furthermore a regulation process of electron transport in the 20S,22R-cholesterol system is considered.
D000325:Adrenodoxin; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002784:Cholesterol; D002846:Chromatography, Affinity; D003577:Cytochrome P-450 Enzyme System / Q000302:isolation & purification; D004579:Electron Transport; D005287:Ferredoxin-NADP Reductase / Q000302:isolation & purification; D008928:Mitochondria / Q000201:enzymology*; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000302:isolation & purification; D013250:Steroid Hydroxylases / Q000302:isolation & purification
D000596:Amino Acids; D000325:Adrenodoxin; D003577:Cytochrome P-450 Enzyme System; D002784:Cholesterol; D013250:Steroid Hydroxylases; D005287:Ferredoxin-NADP Reductase; D009247:NADH, NADPH Oxidoreductases