title: [Stability and catalytic properties of o-diphenol oxidase. 2. Oxidation of monophenols].
abstract: 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.
authors.forename: I A
authors.initials: IA
authors.lastname: Butovich
mesh_terms: 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
chemical_list: D010636:Phenols; D004156:Catechol Oxidase; D014442:Monophenol Monooxygenase
vernacular_title: Stabil'nost' i kataliticheskie svoĭstva o-difenoloksidazy. 2. Okislenie monofenolov.