Chirality in Biological Nanospaces: Reactions in Active Sites

Nilashis Nandi University of Kalyani
Chirality in Biological Nanospaces: Reactions in Active Sites
Publication Type List Price
Reference $119.95 / £76.99
Publication Date Imprint
7/13/2011 CRC Press
Disciplines ISBN
Chemistry 9781439840023
Number of Pages Buy with discount
209 buy


Chiralty 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 Contents


Chirality and chiral discrimination

Enzymes, active site, and vital biological reactions

Chirality and reactions in active sites


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


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


Influence of chirality on the hydrolysis reactions within the active site of hydrolases

Chiral discrimination by epoxide hydrolases

Chiral discrimination by lipases


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


Chiral discrimination in the active site of ligases

Chiral discrimination by germacrene D synthases

Chiral discrimination by aminoacyl-tRNA synthetases


Summary and future



by Editor1 last modified September 22, 2011 - 15:42
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- 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