Almost all metabolic processes in living cells need enzyme catalysis in order to proceed at rates fast enough to sustain life. Although enzyme processes have been investigated for many decades, and more than 5000 have been identified, the extreme complexity of the biochemistry involved has meant that the way in which a particular enzyme operates can be far from clear.
Further reading Wikipedia
A current trend involves focussing on 'electrostatic catalysis' to try and explain how the enzymes have the ultra-specific shapes they have, and which in turn influences their ultra-specific functions.
While the function of enzymes has been well-known to researchers for decades, the driving force behind it is still a hotly debated topic. Herein, we report significant evidence for electrostatics being that driving force, using a simple, computationally inexpensive, multiscale model of monoamine oxidase A and phenylethylamine.
The indispensable role of enzymes in virtually all life processes has inspired researchers for decades. The paramount role of enzymes is their catalytic function. Enzymes facilitate chemical reactions involved in biological processes to occur at significantly higher rates (and, consequently, at milder conditions) than in the plain aqueous environment. While that feature alone represents an enormous research potential, it should be stressed that enzymes are in every imaginable aspect highly complex systems. Consisting typically of thousands of atoms and including flexible domains, the structure of enzymes is governed by a sophisticated network of interactions, and the formation of the structure (folding) and its stability still remains enigmatic, despite significant research efforts on both the experimental and theoretical fronts.
Source : Function of the Monoamine Oxidase A Enzyme Confirmed by Quantum Computations American Chemical Society, Catalysis, 9, 2, 1231â1240
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