Chirality in Biological Nanospaces: Reactions in Active Sites
Nilashis Nandi
University of Kalyani
DescriptionChiralty is widely studied and omnipresent in biological molecules. however, how the retention of enantiomeric forms persists in many life processes with racemization is still unclear, and the molecular understanding of the stringent chiral specificity in enzymatic reactions is sparce.An overview of the influence of chirality in driving reactions within enzymatic cavities, Chirality in Biological Nanospaces: Reactions in Active Sties covers: - Influences of molecular chirality on the structure of the active site and network of interactions to ddrive 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 subtrate molecules Despite being time-consuming and expensive, trial-and-error is often the primary method used to develop synthetic enzymes. The 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. Table of ContentsIntroductionChirality and chiral discrimination Enzymes, active site, and vital biological reactions Chirality and reactions in active sites References Chiral discrimination in the active site of oxidoreductase Cytochrome P450: discrimination in drug (warfarin) interaction Enantioselectivity of hydride transfer of NADPH by alcohol oxidoreductase and conversion of epoxide to β-keto acid by 2-[(R)-2-hydroxypropylthio]-ethanesulfonate dehydrogenase Lipooxygenase and cyclooxygenase: generation of chiral peroxide from achiral polyunsaturated fatty acid Nitric oxide synthase: effects of substrate and cofactors on chiral discrimination for binding the enantiomeric ligands Enoyl reductase: chirality dependent branching of a growing polyketide chain References Transferases and chiral discrimination Peptidyl transferase center within ribosome: peptide bond formation and chiral discrimination Chiral discrimination by telomerase Chiral discrimination by HIV-1 reverse transcriptase Chiral discrimination and nuclear DNA polymerases References Influence of chirality on the hydrolysis reactions within the active site of hydrolases Chiral discrimination by epoxide hydrolases Chiral discrimination by lipases References Influence of chirality on the reactions in the active site of lyases Hydroxynitrile lyases: interaction with chiral substrates Acceptance of both epimers of uronic acid by chondroitin lyase ABC References Chiral discrimination in the active site of ligases Chiral discrimination by germacrene D synthases Chiral discrimination by aminoacyl-tRNA synthetases References Summary and future References Index |
Document ActionsFeatures- Discusses the influence of chirality in active sites in relation to the enzymatic reactions- Discusses the chrial discrimination in most (five out of six) enzyme classes - Introduces the importance of the active site, a biological nanospace, in vital reactions - Provides a molecular perspective on how active site research can be used in effective biocatalysis, biotransformation, novel protein design, and predicting protein function from structure |
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CRC Press — 2010 NanoScience and CleanTech catalog
