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. 1997 Feb;72(2 Pt 1):619–626. doi: 10.1016/s0006-3495(97)78700-9

The Contribution of Electrostatic and van der Waals Interactions to the Stereospecificity of the Reaction Catalyzed by Lactate Dehydrogenase

Jeroen van Beek 1, Robert Callender 1, M R Gunner 1
PMCID: PMC1185589  PMID: 9017191

Abstract

Continuum electrostatic calculations in conjunction with molecular dynamics simulations have been used to investigate the source of the stereospecificity in the hydride transfer reaction catalyzed by lactate dehydrogenase (LDH). These studies show that favorable electrostatic interactions between the carboxamide group of the reduced nicotinamide adenine dinucleotide coenzyme and protein residues of the active site of LDH can account for much if not all of the stereospecificity of the LDH-catalyzed reaction, with A-side hydride transfer more than 107 times greater than B-side transfer. Unfavorable steric interactions within the binding complex for B-side transfer are not found.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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