Mutational Effects on Conformational Energy Landspace of Relatively New NADP+-Dependent FDH: A Molecular Dynamics Study (original) (raw)

Abstract

Formate dehydrogenase (FDH, EC 1.2.1.2) that was first found in pea seeds in 1951 by Davison is one of the widely used enzyme for coenzyme regeneration in the processes of chiral synthesis. The fact that hydride transfer and cofactor binding were the most important rate-limiting steps in the catalytic mechanism of FDH and the absence of proton-release stages that exist in all dehydrogenase catalyzed reactions, considering that formate is structurally the simplest of dehydrogenase substrates, have allowed regarding this reaction as a model to be used in studies of the molecular mechanism [1-2]. Because of the reason that many native FDH’s are highly specific to NAD+ coenzyme, FDH is widely used in regeneration of NADH, it could not been used in NADPH regeneration. In this study, a new formate dehydrogenase, which is obtained from Burckholderia sp. (Bsp383) and the crystal structure has been solved, were used [3]. Contrary to other FDH enzymes, this FDH is NADP+-dependent enzym. In or...

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