Chirality in Biological Nanospaces Reactions in Active Sites

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. An overview of the influence of chirality in driving reactions within enzymatic cavities, Chirality in Biological Nanospaces: Reactions in Active Sites covers: Influences of molecular chirality on the structure of the active site and network of interactions to drive reactions with improved speed, accuracy, and efficiency The conserved features of the organization of the active site structures of enzymes The intricate interplay of electrostatic, hydrophobic, and van der Waals interactions Interactions between the active site residues and the substrate molecules Despite being time-consuming and expensive, trial-and-error is often the primary method used to develop synthetic enzymes. This book describes methods that combine crystallographic studies with electronic structure-based computational analysis. These methods may lead to future elucidation of new drugs that can target biological active sites with better efficacy and can be used to design custom-made novel biocytes with improved efficiency.

IntroductionChirality and chiral discriminationEnzymes, active site, and vital biological reactionsChirality and reactions in active sitesReferencesChiral discrimination in the active site of oxidoreductaseCytochrome P450: discrimination in drug (warfarin) interactionEnantioselectivity of hydride transfer of NADPH by alcohol oxidoreductase and conversion of epoxide to ß-keto acid by 2-[(R)-2-hydroxypropylthio]-ethanesulfonate dehydrogenaseLipooxygenase and cyclooxygenase: generation of chiral peroxide from achiral polyunsaturated fatty acidNitric oxide synthase: effects of substrate and cofactors on chiral discrimination for binding the enantiomeric ligandsEnoyl reductase: chirality dependent branching of a growing polyketide chainReferences Transferases and chiral discriminationPeptidyl transferase center within ribosome: peptide bond formation and chiral discriminationChiral discrimination by telomeraseChiral discrimination by HIV-1 reverse transcriptaseChiral discrimination and nuclear DNA polymerasesReferencesInfluence of chirality on the hydrolysis reactions within the active site of hydrolasesChiral discrimination by epoxide hydrolasesChiral discrimination by lipasesReferencesInfluence of chirality on the reactions in the active site of lyasesHydroxynitrile lyases: interaction with chiral substratesAcceptance of both epimers of uronic acid by chondroitin lyase ABCReferencesChiral discrimination in the active site of ligasesChiral discrimination by germacreneD synthasesChiral discrimination by aminoacyl-tRNA synthetasesReferencesSummary and futureReferencesIndex

Nilashis Nandi was born in Cooch Behar, West Bengal, India (1965). He received his B.Sc. (Hons.) (1983) and M.Sc. (1985) degrees from North Bengal University and Ph.D. (1992) from Visva Bharati University. He became a postdoctoral fellow at the Indian Institute of Science, India (1993–1997), a J.S.P.S. postdoctoral fellow at Nagoya University, Japan (1997–1999), and an Alexander von Humboldt postdoctoral fellow at the Max Planck Institute of Colloids and Interfaces, Germany (1999–2000). Dr. Nandi was a faculty member in the chemistry group of Birla Institute of Technology and Science, Pilani, India from 2001–2007 and became a professor in the Department of Chemistry, University of Kalyani in 2008 where he has worked ever since. His research interest is focused on theoretical and computational studies in biophysical chemistry.