This chapter discusses the enzyme kinetics by means of the Michaelis–Menten kinetics that
goes back to a publication by the German biochemist Leonor Michaelis and Canadian …

Steady-state enzyme kinetics is a cornerstone technique of biochemistry and related
sciences since it allows the characterization and quantification of enzyme behaviour …

The basis of enzyme kinetic modelling was established during the early 1900's when the
work of Leonor Michaelis and Maud Menten produced a pseudo-steady state equation …

Determination of enzyme kinetic parameters for the metabolism of a new chemical entity has
become an important part of the drug discovery and development process. Estimation of …

This chapter will provide a general introduction to the kinetics of enzyme-catalyzed
reactions, including a general discussion of catalysts, reaction rates, and binding constants …

This chapter provides a general introduction to the kinetics of enzyme-catalyzed reactions,
with a focus on drug-metabolizing enzymes. A prerequisite to understanding enzyme …

Selective inhibitors of enzyme‐catalyzed reactions are widely used in both biochemical and
medical science. The inhibitor may be used to block either a single enzyme or a metabolic …

A Large number of pharmacologically important compounds have been found to act as
enzyme inhibitors and a kinetic study of the inhibitory process can provide important …

Clinical Chemistry 51, No. 11, 2005 2219 therapeutic agents has increased with the
mapping of the human genome, which facilitates identification of novel enzyme targets. To …

Publisher Summary This chapter focuses on the fundamental kinetic properties of reactions
catalyzed by enzymes. Monomolecular reactions, that is, single substrate reactions, take …