Chirality Related to Biocatalysis and Enzymes in Organic Synthesis

The production of chiral compounds as single enantiomers in the synthesis of drugs and intermediates is extremely important to the pharmaceutical industry. Due to the stereoselective interactions of a chiral drug with optically active biological macromolecules, two stereoisomeric compounds tend to differ in their pharmacokinetic/pharmacodynamic properties. Indeed, enantiomeric discrimination displayed by metabolizing enzymes often results in a preference for one enantiomer of a chiral drug. Biocatalysis involves the use of enzymes or whole cells that contain the desired enzyme or enzyme system as catalysts for chemical reactions. Baeyer-Villiger oxidation, double bond epoxidation and heteroatom oxidation also fall within the scope of this class of enzyme. As they catalyze redox processes, many of these reactions are freely reversible, and indeed oxidoreductases can also promote the reduction of aldehydes, ketones, carboxylic acids, and double and triple carbon-carbon bonds as well. Biocatalysts are also efficient promoters of synthetically useful carbon-carbon and carbonheteroatom bond-forming reactions.