Structure and function of the l-threonine dehydrogenase (TkTDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis.

@article{Bowyer2009StructureAF,
  title={Structure and function of the l-threonine dehydrogenase (TkTDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis.},
  author={Angela Bowyer and Halina Mikolajek and John W Stuart and Steve P. Wood and Farrukh Jamil and Naeem Rashid and Muhammad Akhtar and Jon B. Cooper},
  journal={Journal of structural biology},
  year={2009},
  volume={168 2},
  pages={294-304}
}
The X-ray structure of the holo-form of l-threonine dehydrogenase (TDH) from Thermococcus kodakaraensis (TkTDH) has been determined at 2.4A resolution. TDH catalyses the NAD(+)-dependent oxidation of l-threonine to 2-amino-3-ketobutyrate, and is one of the first enzymes in this family to be solved by X-ray crystallography. The enzyme is a homo-tetramer, each monomer consisting of 350 amino acids that form two domains; a catalytic domain and a nicotinamide co-factor (NAD(+))-binding domain… CONTINUE READING
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