Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution.

@article{Lindqvist1992ThreedimensionalSO,
  title={Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution.},
  author={Ylva Lindqvist and G. R. Eugenia Schneider and Ulrich Ermler and Mikael Sundstr{\"o}m},
  journal={The EMBO journal},
  year={1992},
  volume={11 7},
  pages={2373-9}
}
The crystal structure of Saccharomyces cerevisiae transketolase, a thiamine diphosphate dependent enzyme, has been determined to 2.5 A resolution. The enzyme is a dimer with the active sites located at the interface between the two identical subunits. The cofactor, vitamin B1 derived thiamine diphosphate, is bound at the interface between the two subunits. The enzyme subunit is built up of three domains of the alpha/beta type. The diphosphate moiety of thiamine diphosphate is bound to the… CONTINUE READING

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