Structure, mechanism and catalytic duality of thiamine-dependent enzymes

@article{Frank2007StructureMA,
  title={Structure, mechanism and catalytic duality of thiamine-dependent enzymes},
  author={Ren{\'e} Frank and Finian J Leeper and Ben F Luisi},
  journal={Cellular and Molecular Life Sciences},
  year={2007},
  volume={64},
  pages={892-905}
}
Thiamine is an essential cofactor that is required for processes of general metabolism amongst all organisms, and it is likely to have played a role in the earliest stages of the evolution of life. Here, we review from a structural perspective the enzymatic mechanisms that involve this cofactor. We explore asymmetry within homodimeric thiamine diphosphate (ThDP)-dependent enzyme structures and discuss how this may be correlated with the kinetic properties of half-of-the-sites reactivity, and… CONTINUE READING
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Structural basis for gene regulation by a thiamine pyrophosphate - sensing riboswitch

  • K. Schrçder-Tittmann, E. Hinze
  • 2006

Structure of the eukaryotic thiamine pyrophosphate riboswitch with its regulatory ligand

  • N. Sudarsan, J. E. Barrick, R. R. Breaker
  • Science
  • 2006

Crystal structure of the free radical intermediate of pyruvate : ferredoxin oxidoreductase

  • R. A. Frank, J. V. Pratap, X. Y. Pei, R. N. Perham, B. F. Luisi
  • Science
  • 2005

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