Re‐engineering the discrimination between the oxidized coenzymes NAD+ and NADP+ in clostridial glutamate dehydrogenase and a thorough reappraisal of the coenzyme specificity of the wild‐type enzyme

@article{Capone2011ReengineeringTD,
  title={Re‐engineering the discrimination between the oxidized coenzymes NAD+ and NADP+ in clostridial glutamate dehydrogenase and a thorough reappraisal of the coenzyme specificity of the wild‐type enzyme},
  author={Marina Capone and David O. Scanlon and Joanna Griffin and Paul C. Engel},
  journal={The FEBS Journal},
  year={2011},
  volume={278}
}
Clostridial glutamate dehydrogenase mutants, designed to accommodate the 2′‐phosphate of disfavoured NADPH, showed the expected large specificity shifts with NAD(P)H. Puzzlingly, similar assays with oxidized cofactors initially revealed little improvement with NADP+, although rates with NAD+ were markedly diminished. This article reveals that the enzyme’s discrimination in favour of NAD+ and against NADP+ had been greatly underestimated and has indeed been abated by a factor of > 16 000 by the… 
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