Quinolinate synthase

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Quinolinate synthase
Identifiers
EC no. 2.5.1.72
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Quinolinate synthase (EC 2.5.1.72, NadA, QS, quinolinate synthetase) is an enzyme with systematic name glycerone phosphate:iminosuccinate alkyltransferase (cyclizing). [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction

glycerone phosphate + iminosuccinate pyridine-2,3-dicarboxylate + 2 H2O + phosphate

This iron-sulfur protein that requires a [4Fe-4S] cluster for activity.

References

  1. ↑ Ollagnier-de Choudens S, Loiseau L, Sanakis Y, Barras F, Fontecave M (July 2005). "Quinolinate synthetase, an iron-sulfur enzyme in NAD biosynthesis" (PDF). FEBS Letters. 579 (17): 3737–43. Bibcode:2005FEBSL.579.3737O. doi: 10.1016/j.febslet.2005.05.065 . PMID   15967443.
  2. ↑ Katoh A, Uenohara K, Akita M, Hashimoto T (July 2006). "Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate and occur in the plastid". Plant Physiology. 141 (3): 851–7. doi:10.1104/pp.106.081091. PMC   1489895 . PMID   16698895.
  3. ↑ Sakuraba H, Tsuge H, Yoneda K, Katunuma N, Ohshima T (July 2005). "Crystal structure of the NAD biosynthetic enzyme quinolinate synthase". The Journal of Biological Chemistry. 280 (29): 26645–8. doi: 10.1074/jbc.C500192200 . PMID   15937336.
  4. ↑ Rousset C, Fontecave M, Ollagnier de Choudens S (August 2008). "The [4Fe-4S] cluster of quinolinate synthase from Escherichia coli: investigation of cluster ligands". FEBS Letters. 582 (19): 2937–44. Bibcode:2008FEBSL.582.2937R. doi: 10.1016/j.febslet.2008.07.032 . PMID   18674537.
  5. ↑ Saunders AH, Booker SJ (August 2008). "Regulation of the activity of Escherichia coli quinolinate synthase by reversible disulfide-bond formation". Biochemistry. 47 (33): 8467–9. doi:10.1021/bi801135y. PMC   3319134 . PMID   18651751.
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