Stereospecific deuteration of 2-deoxyerythrose 4-phosphate using 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase

Rachel M Williamson; Amy L Pietersma; Geoffrey B Jameson; Emily J Parker

doi:10.1016/j.bmcl.2005.02.080

Stereospecific deuteration of 2-deoxyerythrose 4-phosphate using 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase

Bioorg Med Chem Lett. 2005 May 2;15(9):2339-42. doi: 10.1016/j.bmcl.2005.02.080.

Authors

Rachel M Williamson¹, Amy L Pietersma, Geoffrey B Jameson, Emily J Parker

Affiliation

¹ Institute of Fundamental Sciences, Massey University, Palmerston North 5301, New Zealand.

PMID: 15837321
DOI: 10.1016/j.bmcl.2005.02.080

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

3-Deoxy-7-Phosphoheptulonate Synthase / chemistry
3-Deoxy-7-Phosphoheptulonate Synthase / metabolism*
Binding Sites
Catalysis
Deuterium
Indicators and Reagents
Isotope Labeling / methods
Models, Molecular
Protein Conformation
Sugar Phosphates / chemistry
Sugar Phosphates / metabolism*

Substances

Indicators and Reagents
Sugar Phosphates
erythrose 4-phosphate
Deuterium
3-Deoxy-7-Phosphoheptulonate Synthase