quinolinate synthase 2.5.1.72
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Publisher
Springer Berlin Heidelberg
Link
http://link.springer.com/content/pdf/10.1007/978-3-642-36240-8_60
Reference13 articles.
1. Katoh, A.; Uenohara, K.; Akita, M.; Hashimoto, T.: Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate and occur in the plastid. Plant Physiol., 141, 851-857 (2006)
2. Gardner, P.R.; Fridovich, I.: Quinolinate synthetase: the oxygen-sensitive site of de novo NAD(P)+ biosynthesis. Arch. Biochem. Biophys., 284, 106-111 (1991)
3. Saunders, A.H.; Griffiths, A.E.; Lee, K.H.; Cicchillo, R.M.; Tu, L.; Stromberg, J.A.; Krebs, C.; Booker, S.J.: Characterization of quinolinate synthases from Escherichia coli, Mycobacterium tuberculosis, and Pyrococcus horikoshii indicates that [4Fe-4S] clusters are common cofactors throughout this class of enzymes. Biochemistry, 47, 10999-11012 (2008)
4. Saunders, A.H.; Booker, S.J.: Regulation of the activity of Escherichia coli quinolinate synthase by reversible disulfide-bond formation. Biochemistry, 47, 8467-8469 (2008)
5. Marinoni, I.; Nonnis, S.; Monteferrante, C.; Heathcote, P.; Haertig, E.; Boettger, L.H.; Trautwein, A.X.; Negri, A.; Albertini, A.M.; Tedeschi, G.: Characterization of L-aspartate oxidase and quinolinate synthase from Bacillus subtilis. FEBS J., 275, 5090-5107 (2008)
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