Directly and Indirectly Determinable Rate Constants in Michaelian Enzyme-Catalyzed Reactions
$ 42.5
Description
The literature is replete with views and comments about rates, the most popular of which is the catalytic rate constant, often regarded as the turnover number. In most cases, the catalytic rate constant, the cognate maximum velocity of the enzyme biological function, and the Michaelian constant are also regarded as steady-state kinetic parameters. This study refutes that and posits that they are rather mixed-order and zero-order parameters, as the case may be. The study confirmed that there are steps in enzyme-catalyzed reactions, each possessing its own life span with a corresponding first-order rate constant. The study showed that there is pre-activated complex formation, otherwise referred to as "chemistry," an activated complex, otherwise known as the transition state, and a post-transition state leading to product release. The duration or life span of any catalytic cycle is always longer than the life span of any step, and the sum of all the life spans of all the steps is equal to the life span of the catalytic cycle. The findings are believed to be of value as a working guide for the design of appropriate kinetic experiments for both medical (pharmaceutical) and non-medical (industrial) applications.