ABSTRACT
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 physician Maud Menten, who built on earlier experimental findings, e.g., those published by the French physical chemist Victor Henri. The term “enzyme kinetics” is in so far somewhat misleading as one might draw the conclusion from it that the basic principles of chemical kinetics are valid in this area, which is of course not the case. In the field of enzymology the term inhibitor stands for molecules or ions that reduce the rate of a biochemical reaction catalyzed by an enzyme. The biological role of inhibitors, especially non-competitive ones, is to adhere to the special conditions of a given cellular environment. Competitive inhibitors are of widespread clinical use as therapeutics. In case of competitive inhibition, the active site of the enzyme binds either the substrate or the inhibitor but both inhibitor and substrate.
