Summary
Two forms of enzymatic posttranslational modifications of the monooxygenase system are described: modification by phosphatase and modification by protein kinase. Phosphatase treatment of microsomes isolated from phenobarbital-pretreated rabbits and rats caused a marked decrease of monooxygenase activity which was paralleled by a comparable decrease of NADPH-cytochrome P-450 reductase activity while the second essential component of the system, cytochrome P-450, remained unaltered. Thus phosphatase attacks monooxygenase via reductase. Protein kinases showed the opposite preference; while cytochrome P-450 was phosphorylated, NADPH-cytochrome P-450 reductase was not. Thus the kinase affects monooxygenase via cytochrome P-450. The phosphorylation of cytochrome P-450 turned out to be a specific reaction observed only with certain cytochrome P-450 isoenzymes and certain protein kinases.
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Dedicated to Professor E. Hecker on the occasion of his 60th birthday
This work was supported in part by the Deutsche Forschungsgemeinschaft
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Pyerin, W., Horn, F. & Taniguchi, H. Posttranslational modifications of the cytochrome P-450 monooxygenase system. J Cancer Res Clin Oncol 113, 155–159 (1987). https://doi.org/10.1007/BF00391438
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DOI: https://doi.org/10.1007/BF00391438