Investigations concerning the mode of action of 3,4-dihydroxybutyl-1-phosphonate on Escherichia coli.

摘要: Experiments were performed to evaluate the ability of enzymes Escherichia coli involved in glycerol 3-phosphate metabolism recognize phosphonic acid analogues natural substrate. Neither catabolic membrane-bound glycerol-3-phosphate dehydrogenase nor acyl coenzyme A: acyltransferase can use 3,4-dihydroxybutyl-1-phosphnate or 2,3-dihydroxypropyl-1-phosphonate are inhibitors reduction dihydroxyactone phosphate as substrates. The 4-carbon analogue does not exhibit inhibitory activity for either these enzymes. While 3-carbon has no effect upon dehydrogenase, it appear have a slight but reproducible on acyltransferase. Glycerol and 3,4-dihydroxybutyl-1-phosphonate by 3-phosphate:NAD (P) oxidoreductase. rac-2,3-Dihydroxypropyl-1-phosphonate be recognized this enzyme. apparent K-i snglycerol is 19 muM D-3,4-dihydroxybutyl-1-phosphonate 42 muM. In addition 3-phosphate:NAD(P) oxidoreductase catalyzes 4-hydroxy-3-oxobutyl-1-phosphonate (apparent K-m 182 muM), dihydroxyacetone phosphate. 3,4-Dihydroxybutyl-1-phosphonate both competitive inhibitor Ki 740 muM) substrate 450 CDP-diglyceride: 3 phosphatidyltransferase CDP-diglyceride:L-serine phosphatidyltransferase. relationship ofthese vitro studies vivo investigations discussed.