Racemic 2-deoxyerythrose 4-phosphate was synthesized and one enantiomer of this compound was found to be a substrate for Escherichia coli 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase, the first enzyme of the shikimate pathway. When the reaction was carried out in deuterium oxide, an enzyme-catalyzed regio- and stereoselective incorporation of deuterium into the product was observed.
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Investigating the role of the hydroxyl groups of substrate erythrose 4-phosphate in the reaction catalysed by the first enzyme of the shikimate pathway.
Bioorg Med Chem Lett
November 2011
Biomolecular Interaction Centre and Department of Chemistry, University of Canterbury, Private Bag 4800, Christchurch 8140, New Zealand.
3-Deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) synthase catalyses the first step of the shikimate pathway, which is responsible for the biosynthesis of aromatic amino acids in microorganisms and plants. This enzyme catalyses an aldol reaction between phosphoenolpyruvate and D-erythrose 4-phosphate to generate DAH7P. Both 2-deoxyerythrose 4-phosphate and 3-deoxyerythrose 4-phosphate were synthesised and tested as alternative substrates for the enzyme.
View Article and Find Full Text PDFMechanistic divergence of two closely related aldol-like enzyme-catalysed reactions.
Org Biomol Chem
November 2005
Institute of Fundamental Sciences, Massey University, Private Bag 11-222, Palmerston North, New Zealand.
The analysis of the interaction of threose 4-phosphate and 2-deoxyerythrose 4-phosphate with 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAH7PS) reveals previously unrecognised mechanistic differences between the DAH7PS-catalysed reaction and that catalysed by the closely related enzyme, 3-deoxy-D-manno-octulosonate 8-phosphate synthase (KDO8PS).
View Article and Find Full Text PDFStereospecific deuteration of 2-deoxyerythrose 4-phosphate using 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase.
Bioorg Med Chem Lett
May 2005
Institute of Fundamental Sciences, Massey University, Palmerston North 5301, New Zealand.
Racemic 2-deoxyerythrose 4-phosphate was synthesized and one enantiomer of this compound was found to be a substrate for Escherichia coli 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase, the first enzyme of the shikimate pathway. When the reaction was carried out in deuterium oxide, an enzyme-catalyzed regio- and stereoselective incorporation of deuterium into the product was observed.
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