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- W2019014987 abstract "The mutant E270A of Thermus thermophilus 3-isopropylmalate dehydrogenase exhibits largely reduced (∼1%) catalytic activity and negligible activation by K(+) compared to the wild-type enzyme. A 3-4 kcal/mol increase in the activation energy of the catalysed reaction upon this mutation could also be predicted by QM/MM calculations. In the X-ray structure of the E270A mutant a water molecule was observed to take the place of K(+). SAXS and FRET experiments revealed the essential role of E270 in stabilisation of the active domain-closed conformation of the enzyme. In addition, E270 seems to position K(+) into close proximity of the nicotinamide ring of NAD(+) and the electron-withdrawing effect of K(+) may help to polarise the aromatic ring in order to aid the hydride-transfer." @default.
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- W2019014987 date "2014-12-10" @default.
- W2019014987 modified "2023-10-05" @default.
- W2019014987 title "Glutamate 270 plays an essential role in K<sup>+</sup>-activation and domain closure of<i>Thermus thermophilus</i>isopropylmalate dehydrogenase" @default.
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- W2019014987 doi "https://doi.org/10.1016/j.febslet.2014.12.005" @default.
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