ABSTRACT
This chapter examines the overall kinetics of enzyme-catalyzed reactions in which there is net conversion of substrate to product and presents the simplest possible scheme involving one substrate and one product. Steady-state kinetic analysis provides a useful overview of enzyme activity. Reactions involving the transfer of electrons or hydride ions during enzyme catalysis are likely to involve tunnelling. Steady-state kinetics provides a sensitive way of determining the binding of ligands, other than the substrate(s) itself, if they have an effect on the observed velocity of the reaction. Conclusions from steady-state kinetic analyse are best confirmed by direct analysis of inhibitor binding to the enzyme in the absence and presence of substrate using transient kinetic methods. Cooperative interactions, in the classical sense, refer to ligand binding to a multisite protein, such that binding of the first ligand molecule affects the binding of subsequent identical ligand molecules, either positively or negatively.
