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Biosynthesis in Escherichia coli of sn-glycerol-3-phosphate, a precursor of phospholipid. Further kinetic characterization of wild type and feedback-resistant forms of the biosynthetic sn-glycerol-3-phosphate dehydrogenase
1980
Journal of Biological Chemistry
Homogeneous wild type and feedback-resistant forms of the biosynthetic glycerol-3-phosphate dehydrogenase (NAD+) of Escherichia coli (EC 1.1.1.8) were employed for studies of substrate and inhibitor specificity. The phosphonate analog of dihydroxyacetone-P, 4-hydroxy-3-oxybutyl 1-phosphonate, and glycolaldehyde phosphate proved to be substrates of both enzymes. NADPH, NADH, and nicotinamide hypoxanthine dinucleotide were used as substrates about equally well by both enzymes. Both enzymes were
pmid:6767719
fatcat:mmxl4ssftjhunevpipzn4mpfma