Enzymatic in situ analysis by 1H-NMR of the hydrogen transfer stereospecificity of NAD(P)+-dependent dehydrogenases.

@article{Nakajima1989EnzymaticIS,
  title={Enzymatic in situ analysis by 1H-NMR of the hydrogen transfer stereospecificity of NAD(P)+-dependent dehydrogenases.},
  author={Nobuyoshi Nakajima and Kazuo Nakamura and Nobuyoshi Esaki and Hiroyuki Tanaka and Kenji Soda},
  journal={Journal of biochemistry},
  year={1989},
  volume={106 3},
  pages={515-7}
}
We have established a simple procedure for the in situ analysis of stereospecificity of an NAD(P)-dependent dehydrogenase for C-4 hydrogen transfer of NAD(P)H by means of glutamate racemase [EC 5.1.13] and glutamate dehydrogenase [EC 1.4.1.3]. Glutamate racemase inherently catalyzes the exchange of alpha-H of glutamate with 2H during racemization in 2H2O. When the reactions of glutamate racemase and glutamate dehydrogenase, which is pro-S specific for the C4-H transfer of NAD(P)H, are coupled… CONTINUE READING

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