[Hydroxylation of aniline and aminoantipyrine derivatives (1-phenyl-2,3-dimethylaminopyrazolon-5) in liver endoplasmic reticulum].
The absence of correlation between the effect of aniline and aminoantipyrine derivatives on cytochrome P-450 reduction rate and its oxidation rate draw to the conclusion that the reductase reaction is not a limiting step of hydroxylation for all substrates. Km is found to be directly proportional to Vmax of hydroxylated substrates. Hence, in these reactions the Km value is determined not by the value Ks but by the kappa+2/kappa+1 ratio. Km is not a characteristic of the affinity of cytochrome P-450 to substrates. The calculations were made to show that cytochrome P-450 formed two types of the enzyme-substrate complexes containing one or two substrate molecules. The complex in which one molecule of cytochrome P-450 binds one substrate molecule is considered to be active.
D000632:Aminopyrine / Q000378:metabolism*; D000693:Anaerobiosis; D000818:Animals; D000983:Antipyrine / Q000378:metabolism; D002458:Cell Fractionation; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006900:Hydroxylation; D007700:Kinetics; D008099:Liver / Q000166:cytology* / Q000378:metabolism; D008297:Male; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism; D051381:Rats; D013053:Spectrophotometry
D000632:Aminopyrine; D003577:Cytochrome P-450 Enzyme System; D009247:NADH, NADPH Oxidoreductases; D000983:Antipyrine
Gidroksilirovanie proizvodnykh anilina i aminoantipirina (1-fenile-2,3-dimetilaminopirazolon-5) v éndoplazmaticheskom retikulume pecheni