A new perspective on thiamine catalysis.
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.
Pohl
Martina
M
Institute of Molecular Enzyme Technology, University of Duesseldorf, Research Centre Juelich, 52426 Juelich, Germany. ma.pohl@fz-juelich.de
Sprenger
Georg A
GA
Müller
Michael
M
D001419:Bacteria / Q000378:metabolism*; D002384:Catalysis; D008025:Ligases / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D008190:Lyases / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000737:chemistry / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology*; D013835:Thiamine Pyrophosphate / Q000737:chemistry / Q000378:metabolism*
D009097:Multienzyme Complexes; D008190:Lyases; D008025:Ligases; D013835:Thiamine Pyrophosphate