The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography.

@article{Wille2006TheCC,
  title={The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography.},
  author={Georg Wille and Danilo Meyer and Andrea Steinmetz and Erik Hinze and Ralph Peter Golbik and Kai Tittmann},
  journal={Nature chemical biology},
  year={2006},
  volume={2 6},
  pages={324-8}
}
Enzymes that use the cofactor thiamin diphosphate (ThDP, 1), the biologically active form of vitamin B(1), are involved in numerous metabolic pathways in all organisms. Although a theory of the cofactor's underlying reaction mechanism has been established over the last five decades, the three-dimensional structures of most major reaction intermediates of ThDP enzymes have remained elusive. Here, we report the X-ray structures of key intermediates in the oxidative decarboxylation of pyruvate, a… CONTINUE READING

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