ON TRUE AND APPARENT MICHAELIS CONSTANTS IN ENZYMOLOGY. I. DIFFERENCES
Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
Differences between both true and apparent rate constants and Michaelis constants have been examined. Rate constants of elementary stages of real mechanisms are true ones. True Michaelis constant Km is expressed by equation Km = (k-1 + k2)/k1. True constants may be determined for reliable mechanism only for which the equation of initial rate was obtained which displays physical sense of these constants and permits to find the method of their calculation. The true constant values are independent of concentration of reactants, activators, inhibitors, extraneous agents and pH.
The apparent rate constants are such constants of the composite reaction which are observed when this reaction is described by the equation of simple reaction. Michaelis constant calculated by a half of the ultimate constant is an apparent constant. The apparent constants may be functions of several true rate constants and/or concentrations of reacting substances. The evident physical sense of apparent constants being absent, only formal relation between the reaction rate and reactant concentration independent of the investigated mechanism is provided.
Key words: enzyme kinetics, Michaelis-Menten equation, Michaelis constant, limiting rate, substrate constant.
The original article in Russian is available for download in PDF format.
© The Ukrainian Biochemical Journal