Structural, kinetic and computational investigation of Vitis vinifera DHDPS reveals new insight into the mechanism of lysine-mediated allosteric inhibition

@article{Atkinson2013StructuralKA,
  title={Structural, kinetic and computational investigation of Vitis vinifera DHDPS reveals new insight into the mechanism of lysine-mediated allosteric inhibition},
  author={Sarah C Atkinson and C. Dogovski and M. Downton and P. Czabotar and R. Dobson and J. Gerrard and J. Wagner and M. Perugini},
  journal={Plant Molecular Biology},
  year={2013},
  volume={81},
  pages={431-446}
}
Lysine is one of the most limiting amino acids in plants and its biosynthesis is carefully regulated through inhibition of the first committed step in the pathway catalyzed by dihydrodipicolinate synthase (DHDPS). This is mediated via a feedback mechanism involving the binding of lysine to the allosteric cleft of DHDPS. However, the precise allosteric mechanism is yet to be defined. We present a thorough enzyme kinetic and thermodynamic analysis of lysine inhibition of DHDPS from the common… Expand
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