The contribution of electrostatic and van der Waals interactions to the stereospecificity of the reaction catalyzed by lactate dehydrogenase

Jeroen Van Beek, Robert Callender, M. R. Gunner

Research output: Contribution to journalArticle

13 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)619-626
Number of pages8
JournalBiophysical Journal
Volume72
Issue number2 I
StatePublished - Feb 1997

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Static Electricity
L-Lactate Dehydrogenase
Coenzymes
Molecular Dynamics Simulation
NAD
Catalytic Domain
Proteins

ASJC Scopus subject areas

  • Biophysics

Cite this

The contribution of electrostatic and van der Waals interactions to the stereospecificity of the reaction catalyzed by lactate dehydrogenase. / Van Beek, Jeroen; Callender, Robert; Gunner, M. R.

In: Biophysical Journal, Vol. 72, No. 2 I, 02.1997, p. 619-626.

Research output: Contribution to journalArticle

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