[On true and apparent Michaelis constants in enzymology. II. Is the equation k(m)app = k(s) + k)cat)/k(1) true for enzyme-catalysed reactions with activator participation?].
The article is dedicated to analysis of equation which expresses apparent Michaelis constant K(m)app) of enzyme-catalysed reactions with activator participation by means of the substrate constant K(s) and rate constant of enzyme-substrate complex decomposition k(cat). It has been shown that although it is possible to record the mechanisms of such reactions as a scheme similar to Michaelis-Menten model and to derive equation of apparent Michaelis constant as K(m(app) = K(s) + k(cat)/k(1), but this approach cannot be used for investigation of all reactions with activator participation. The equation mentioned above is not obeyed in the general case, it may be true for some mechanisms only or under certain ratio of kinetic parameters of enzyme-catalysed reactions.
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Karakhim
D055162:Biocatalysis; D001671:Biochemistry / Q000379:methods / Q000592:standards*; D004789:Enzyme Activation; D006735:Horseradish Peroxidase / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism; D007700:Kinetics; D012394:Rosaniline Dyes / Q000378:metabolism
D012394:Rosaniline Dyes; C005095:malachite green; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase