[Stability and catalytic properties of o-diphenol oxidase. 2. Oxidation of monophenols].
o-Diphenoloxidase from potato tubers is shown to be a hysteretic enzyme which is dimerized during monophenol oxidation. A diagram of the enzyme activation is suggested. It is established that the enzyme activity in reactions of monophenols oxidation is determined by the nature of substituents in the substrate molecule; the higher phenol acidity, the worse its enzymic oxidation. The effect of substituents in the phenol molecule on the enzymic reaction rate may be described in terms of the Hammet equation.
Butovich
I A
IA
D002384:Catalysis; D004156:Catechol Oxidase / Q000378:metabolism*; D004789:Enzyme Activation; D007700:Kinetics; D014442:Monophenol Monooxygenase / Q000378:metabolism*; D010084:Oxidation-Reduction; D010636:Phenols / Q000378:metabolism*; D013379:Substrate Specificity
D010636:Phenols; D004156:Catechol Oxidase; D014442:Monophenol Monooxygenase
Stabil'nost' i kataliticheskie svoĭstva o-difenoloksidazy. 2. Okislenie monofenolov.