Equations known as rate law link the consumption of the reactants, an observable, to the kinetics of a reaction. The rate is influenced by the reactant concentrations, their thermodynamics, and the precise mechanism of the reaction.
The second-order rate constant kinact/KI (also known as the covalent efficiency constant) explains both the affinity of the initial reversible encounter complex and the maximum rate of covalent bond formation. In the context of enzyme-substrate kinetics, it is comparable to the enzyme specificity constant kcat/KM.
A rate law illustrates how a chemical reaction's rate is influenced by the reactant's concentration. The rate rule for a reaction like aA products typically has the form rate = k[A]n.
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