Abstract
Recent data show that besides the well-known long-term regulation of cytochrome P450-dependent monooxygenase activity by induction there also exists a fast regulation by phosphorylation. This phosphorylation occurs when purified cytochromes P450 are combined with purified protein kinases, and also in intact cells. This process is donor- and acceptor-selective leading to phosphorylation of defined isoenzymes by defined protein kinases. This in turn leads to fast and marked changes in metabolism which are selective for given substrates and regio- and stereo-selective for given positions. This in turn is selectively and differentially influenced by the individual control of the protein kinase in question.
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To facilitate it for the reader to follow the relatively complicated cytochrome P450 nomenclature, the individual isoenzymes are (as far as possible) designated by the recommended nomenclature for their (probable) genes (Nebert et al. 1987) followed in brackets by a relatively simple and relatively widely used one letter nomenclature (Bandiera et al. 1985) and — at there first occurrence in paper — very briefly characterized.
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Oesch-Bartlomowicz, B., Oesch, F. Phosphorylation of cytochrome P450 isoenzymes in intact hepatocytes and its importance for their function in metabolic processes. Arch Toxicol 64, 257–261 (1990). https://doi.org/10.1007/BF01972984
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DOI: https://doi.org/10.1007/BF01972984