A new perspective on thiamine catalysis

Curr Opin Biotechnol. 2004 Aug;15(4):335-42. doi: 10.1016/j.copbio.2004.06.002.

Abstract

Our knowledge of thiamine-catalyzed ligase and lyase reactions has entered a new dimension. Significant achievements have been made in the field of enzymatic catalysis with the detection of hitherto unknown reaction types - extending the synthetic potential of known thiamine diphosphate (ThDP)-dependent enzymes - and the identification and characterization of new enzymes. As we learn more about ThDP-dependent enzymes, we find an ever-expanding range of reactions that they are able to catalyze and see increased amino acid sequence heterogeneity. By contrast, the three-dimensional structures of these enzymes, so far, seem to be highly similar. Non-enzymatic thiazolium and triazolium catalysts have also been developed, enhancing the scope of acyl anion chemistry.

Publication types

  • Review

MeSH terms

  • Bacteria / metabolism*
  • Catalysis
  • Ligases / chemistry*
  • Ligases / classification
  • Ligases / metabolism*
  • Lyases / chemistry*
  • Lyases / classification
  • Lyases / metabolism*
  • Multienzyme Complexes / chemistry
  • Multienzyme Complexes / metabolism
  • Signal Transduction / physiology*
  • Thiamine Pyrophosphate / chemistry
  • Thiamine Pyrophosphate / metabolism*

Substances

  • Multienzyme Complexes
  • Lyases
  • Ligases
  • Thiamine Pyrophosphate