6533b7ddfe1ef96bd12752a9

RESEARCH PRODUCT

Phosphorylation of rabbit liver cytochrome P-450 LM2 and its effect on monooxygenase activity

F. OeschF. OeschA. StierA. StierH. TaniguchiH. TaniguchiW. PyerinW. PyerinC.r. Wolf

subject

CytochromeProtein subunitBiophysicsBiochemistryMixed Function OxygenasesCytochrome P-450 Enzyme SystemmedicineAnimalsPhosphorylationProtein kinase AMolecular Biologychemistry.chemical_classificationbiologyKinaseCell BiologyMolecular biologyKineticsEnzymechemistryBiochemistryPhenobarbitalMicrosomes Liverbiology.proteinMicrosomePhosphorylationRabbitsBenzphetamineProtein Kinasesmedicine.drug

description

The phosphorylation of rabbit liver microsomal cytochrome P-450 LM2 by catalytic subunit of cyclic AMP-dependent protein kinase (W. Pyerin et al. (1983) Carcinogenesis 4, 573) has now been studied in detail with purified soluble form of cytochrome P-450 as well as with the purified protein incorporated into model membranes. The apparent Km values for P-450 of the phosphorylation reaction in all experimental systems were in a range of 2-8 microM, while the Vmax values were dependent on the state of P-450. Upon phosphorylation, the reconstituted enzyme activities with benzphetamine (N-demethylation) and 7-ethoxycoumarin (O-deethylation) as substrates were reduced to 30-40% of control.

yearjournalcountryeditionlanguage
1984-07-31Biochemical and Biophysical Research Communications
https://doi.org/10.1016/s0006-291x(84)80078-9