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 language||English (US)|
|Number of pages||8|
|Issue number||2 I|
|State||Published - Feb 1997|
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