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Curr Opin Biotechnol. 2004 Aug;15(4):335-42.

A new perspective on thiamine catalysis.

Author information

1
Institute of Molecular Enzyme Technology, University of Duesseldorf, Research Centre Juelich, 52426 Juelich, Germany. ma.pohl@fz-juelich.de

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.

PMID:
15296931
DOI:
10.1016/j.copbio.2004.06.002
[Indexed for MEDLINE]
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