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.
Institute of Molecular Enzyme Technology, University of Duesseldorf, Research Centre Juelich, 52426 Juelich, Germany. ma.pohl@fz-juelich.de
Martina
M
Pohl
Georg A
GA
Sprenger
Michael
M
Müller
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