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In contrast to the wellknown regulation of cytochromeP450 (CYP) activity by enzyme induction, which represents a process with slowonset and slow offset, more recent studies revealed phosphorylation as a fast(within observation instantaneous) and isoenzymeselective regulation. Thephosphorylated enzyme (investigated isozyme: CYP2B1) was fully inactive. Thephosphorylation is mediated by PKA and hence under control of hormones anddrugs that alter cellular cAMP levels. The consequences for the metaboliccontrol of toxic species derived from drugs and environmental carcinogens arediscussed. This information will help to improve therapy with drugs metabolizedby CYPs which are phosphorylated by PKA, especially if these drugs possess anarrow window between required effectiveness and unacceptable toxicity.

Fast Regulation of Cytochrome P450 Activities by Phosphorylation and Consequences for Drug Metabolism and Toxicity