6533b855fe1ef96bd12b14d9

RESEARCH PRODUCT

Phosphorylation of cytochrome P450 isoenzymes in intact hepatocytes and its importance for their function in metabolic processes.

Barbara Oesch-bartlomowiczFranz Oesch

subject

chemistry.chemical_classificationCytochromebiologyKinaseHealth Toxicology and MutagenesisCytochrome P450General MedicineMetabolismToxicologyIsoenzymesEnzymeBiochemistrychemistryCytochrome P-450 Enzyme SystemLiverbiology.proteinPhosphorylationAnimalsHumansProtein phosphorylationPhosphorylationProtein kinase A

description

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.

10.1007/bf01972984https://pubmed.ncbi.nlm.nih.gov/2201273