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Gene Review

nadA  -  quinolinate synthase, subunit A

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0739, JW0733, nicA
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Disease relevance of nadA

  • Finally, our data definitely exclude the possibility that other enzymes are involved in the biosynthesis of quinolinic acid in E. coli, since it is possible to synthesize quinolinic acid from l-aspartate, dihydroxyacetone phosphate, and O(2) by using only nadA and nadB gene overexpressed products [1].
  • This sequence, together with the effect of the Fe(II)-chelating agents, suggests that the O2-sensitive site of quinolinate synthetase is an iron-sulfur cluster which is essential for the dehydration reaction catalyzed by the A protein [2].

High impact information on nadA


Chemical compound and disease context of nadA


Biological context of nadA

  • Iron-requiring mutant of Escherichia coli carrying a deletion in the aroG-nadA region of the chromosome [10].
  • Restriction analysis and complementation studies indicated that plasmid pJC778 carried genes nadA, lkyB and sucA which mapped at min 16.5; the lkyB+ allele was dominant over the lkyB207 mutant allele [11].

Associations of nadA with chemical compounds


  1. Cloning, overexpression, and purification of Escherichia coli quinolinate synthetase. Ceciliani, F., Caramori, T., Ronchi, S., Tedeschi, G., Mortarino, M., Galizzi, A. Protein Expr. Purif. (2000) [Pubmed]
  2. Quinolinate synthetase: the oxygen-sensitive site of de novo NAD(P)+ biosynthesis. Gardner, P.R., Fridovich, I. Arch. Biochem. Biophys. (1991) [Pubmed]
  3. L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase. Nasu, S., Wicks, F.D., Gholson, R.K. J. Biol. Chem. (1982) [Pubmed]
  4. Escherichia coli quinolinate synthetase does indeed harbor a [4Fe-4S] cluster. Cicchillo, R.M., Tu, L., Stromberg, J.A., Hoffart, L.M., Krebs, C., Booker, S.J. J. Am. Chem. Soc. (2005) [Pubmed]
  5. Protein A of quinolinate synthetase is the site of oxygen poisoning of pyridine nucleotide coenzyme synthesis in Escherichia coli. Draczynska-Lusiak, B., Brown, O.R. Free Radic. Biol. Med. (1992) [Pubmed]
  6. Modification of aspartate before its condensation with dihydroxyacetone phosphate during quinolinic acid formation in Escherichia coli. Steiner, B.M., Heard, J.T., Tritz, G.J. J. Bacteriol. (1980) [Pubmed]
  7. Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB. Flachmann, R., Kunz, N., Seifert, J., Gütlich, M., Wientjes, F.J., Läufer, A., Gassen, H.G. Eur. J. Biochem. (1988) [Pubmed]
  8. Quinolinate synthetase, an iron-sulfur enzyme in NAD biosynthesis. Ollagnier-de Choudens, S., Loiseau, L., Sanakis, Y., Barras, F., Fontecave, M. FEBS Lett. (2005) [Pubmed]
  9. The mammalian enzyme which replaces B protein of E. coli quinolinate synthetase is D-aspartate oxidase. Nasu, S., Wicks, F.D., Gholson, R.K. Biochim. Biophys. Acta (1982) [Pubmed]
  10. Iron-requiring mutant of Escherichia coli carrying a deletion in the aroG-nadA region of the chromosome. Nagy, J., Dénes, G. J. Bacteriol. (1976) [Pubmed]
  11. Cloning of the lkyB (tolB) gene of Escherichia coli K12 and characterization of its product. Lazzaroni, J.C., Fognini-Lefebvre, N., Portalier, R.C. Mol. Gen. Genet. (1986) [Pubmed]
  12. Mapping and characterization of the nad genes in Salmonella typhimurium LT-2. Foster, J.W., Moat, A.G. J. Bacteriol. (1978) [Pubmed]
  13. Studies on the de novo biosynthesis of NAD in Escherichia coli. The separation of the nadB gene product from the nadA gene product and its purification. Griffith, G.R., Chandler, J.L., Gholson, R.K. Eur. J. Biochem. (1975) [Pubmed]
  14. Pyridine nucleotide cycle of Salmonella typhimurium: isolation and characterization of pncA, pncB, and pncC mutants and utilization of exogenous nicotinamide adenine dinucleotide. Foster, J.W., Kinney, D.M., Moat, A.G. J. Bacteriol. (1979) [Pubmed]
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