Phosphatase affects microsomal monooxygenase mainly via reductase.
Treatment with alkaline phosphatase of hepatic microsomes prepared from rabbit, rat, and mouse caused a marked decrease of their specific monooxygenase activity (7-ethoxycoumarin-deethylation). This decrease occurred without a significant change in the microsomal content of cytochrome P-450, but with an equally marked decrease of NADPH-cytochrome P-450 reductase (cytochrome c reduction). Thus the phosphatase effect on monooxygenase is mainly due to the inactivation of the reductase.
D015660:7-Alkoxycoumarin O-Dealkylase; D000469:Alkaline Phosphatase / Q000494:pharmacology*; D000818:Animals; D003577:Cytochrome P-450 Enzyme System; D066298:In Vitro Techniques; D051379:Mice; D008862:Microsomes, Liver / Q000187:drug effects* / Q000201:enzymology; D009251:NADPH-Ferrihemoprotein Reductase / Q000037:antagonists & inhibitors*; D010105:Oxygenases / Q000037:antagonists & inhibitors*; D011817:Rabbits; D051381:Rats
D003577:Cytochrome P-450 Enzyme System; D010105:Oxygenases; D015660:7-Alkoxycoumarin O-Dealkylase; D009251:NADPH-Ferrihemoprotein Reductase; D000469:Alkaline Phosphatase