6533b855fe1ef96bd12b14d9
RESEARCH PRODUCT
Phosphorylation of cytochrome P450 isoenzymes in intact hepatocytes and its importance for their function in metabolic processes.
Barbara Oesch-bartlomowiczFranz Oeschsubject
chemistry.chemical_classificationCytochromebiologyKinaseHealth Toxicology and MutagenesisCytochrome P450General MedicineMetabolismToxicologyIsoenzymesEnzymeBiochemistrychemistryCytochrome P-450 Enzyme SystemLiverbiology.proteinPhosphorylationAnimalsHumansProtein phosphorylationPhosphorylationProtein kinase Adescription
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.
year | journal | country | edition | language |
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1990-06-01 | Archives of toxicology |