Stereospecific deuteration of 2-deoxyerythrose 4-phosphate using 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase.
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.
Williamson
Rachel M
RM
Institute of Fundamental Sciences, Massey University, Palmerston North 5301, New Zealand.
Pietersma
Amy L
AL
Jameson
Geoffrey B
GB
Parker
Emily J
EJ
D010723:3-Deoxy-7-Phosphoheptulonate Synthase / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D002384:Catalysis; D003903:Deuterium; D007202:Indicators and Reagents; D007553:Isotope Labeling / Q000379:methods; D008958:Models, Molecular; D011487:Protein Conformation; D013403:Sugar Phosphates / Q000737:chemistry / Q000378:metabolism*
D007202:Indicators and Reagents; D013403:Sugar Phosphates; C026959:erythrose 4-phosphate; D003903:Deuterium; D010723:3-Deoxy-7-Phosphoheptulonate Synthase