Chirality in Biological Nanospaces

Chirality in Biological Nanospaces: Reactions in Active Sites

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Features

      • Discusses the influence of chirality in active sites in relation to the enzymatic reactions
      • Discusses the chiral 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

      Summary

      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.

      Table of Contents

      Introduction
      Chirality 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

      Author Bio(s)

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