ABSTRACT
Rates of enzyme-catalyzed reactions are influenced by a number of experimental parameters. Among these parameters are substrate concentration, enzyme concentration, pH, temperature, presence of activators and inhibitors, dielectric constant, and ionic strength of solvent. As the substrate concentration is increased, more and more enzyme molecules are combined with substrate until finally, at high concentration, all enzyme molecules are so combine. However, consider the possibility that when a substrate is bound in one of the active sites, it influences one or more of the remaining active sites, so that the second substrate molecule is bound with a different affinity. This possibility can be extended to include an effect on the rate of transformation of reactants to products. The King-Altman method can be applied to multisubstrate-enzyme-catalyzed reactions as well as one-substrate reactions. There are two intermediates, EA and EX, in the reaction, EA is the Michaelis–Menten complex, but no assumptions are made as to the nature of EX.
