Evidence for an intermediate in quinolinate biosynthesis in Escherichia coli.
Evidence for the formation of an unstable intermediate in the synthesis of quinolinate from aspartate and dihydroxyacetone phosphate by Escherichia coli was obtained using toluenized cells of nadA and nadB mutants of this organism and partially purified A and B proteins in dialysis and membrane cone experiments. The results of these experiments indicate that the nadB gene product forms an unstable compound from aspartate in the presence of flavine adenine dinucleotide, and that this compound is then condensed with dihydroxyacetone phosphate to form quinolinate in a reaction catalyzed by the nadA gene product.
D001224:Aspartic Acid / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D004099:Dihydroxyacetone Phosphate / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D011725:Pyridines / Q000378:metabolism*; D011805:Quinolinic Acids / Q000378:metabolism*
D001426:Bacterial Proteins; D011725:Pyridines; D011805:Quinolinic Acids; D005182:Flavin-Adenine Dinucleotide; D001224:Aspartic Acid; D004099:Dihydroxyacetone Phosphate