Chirality is widely studied and omnipresent in biological molecules. However, how the retention of enantiomeric forms persists in many life processes without racemization is still unclear, and the molecular understanding of the stringent chiral specificity in enzymatic reactions is sparse. Vital life processes occur within the active sites of large biological macromolecules such as proteins, nucleic acids, and lipids. These nanodimensional structures greatly accelerate biological reactions. The chirality of the reactants also has a strong influence on the process, but its importance in such biological reactions has only recently begun to be understood. This book explores the influence of chirality on reaction mechanisms in such biological nanospaces. The text addresses the influence of the chirality of amino acid and sugar in the active sites of transferase, oxidoreductases, hydrolases, lysases, isomerase, ligases, and other systems. It also covers ribosomal architecture.
