A new perspective on thiamine catalysis.

Martina Pohl, Georg A Sprenger, Michael Müller

Journal: Current opinion in biotechnology 2005;15(4):335-42

PMID: 15296931

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.

Address: Institute of Molecular Enzyme Technology, University of Duesseldorf, Research Centre Juelich, 52426 Juelich, Germany. [email protected]

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