Origins of Enzyme Catalytic Power

Abstract

Understanding enzyme function is an exciting research because diverse and often unpredictable solutions are developed to perform seemingly impossible tasks. Enzymes are such powerful catalysts as they lower the height of the activation energy barrier. How do enzymes bring about this decrease in ΔG^≠? Many excellent attempts to dissect this into discrete enthalpic and entropic factors have been made. Rate accelerations are favored when enzyme specifically binds and assembles substrates at the active site and then provides optimal arrangement of catalytic groups. This is clearly an entropic (ΔS^≠) contribution. Stabilization of transition state through enthalpic (ΔH^≠) factors like select hydrogen bonds, salt links, acid–base groups, covalent interactions, etc., is another feature. Various tricks that enzymes employ in achieving catalytic prowess are shown in Fig. 6.1. These components are best understood through case studies, and we will do this through representative examples for each.