Quinolinate synthase
Quinolinate synthase (EC 2.5.1.72, NadA, QS, quinolinate synthetase) is an enzyme with system 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
- ↑ Ollagnier-de Choudens, S., Loiseau, L., Sanakis, Y., Barras, F. and Fontecave, M. (2005). "Quinolinate synthetase, an iron-sulfur enzyme in NAD biosynthesis". FEBS Lett. 579 (17): 3737–3743. doi:10.1016/j.febslet.2005.05.065. PMID 15967443.
- ↑ Katoh, A., Uenohara, K., Akita, M. and Hashimoto, T. (2006). "Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate and occur in the plastid". Plant Physiol. 141 (3): 851–857. doi:10.1104/pp.106.081091. PMC 1489895. PMID 16698895.
- ↑ Sakuraba, H., Tsuge, H., Yoneda, K., Katunuma, N. and Ohshima, T. (2005). "Crystal structure of the NAD biosynthetic enzyme quinolinate synthase". J. Biol. Chem. 280 (29): 26645–26648. doi:10.1074/jbc.C500192200. PMID 15937336.
- ↑ Rousset, C., Fontecave, M. and Ollagnier de Choudens, S. (2008). "The [4Fe-4S] cluster of quinolinate synthase from Escherichia coli: Investigation of cluster ligands". FEBS Lett. 582 (19): 2937–2944. doi:10.1016/j.febslet.2008.07.032. PMID 18674537.
- ↑ Saunders, A.H. and Booker, S.J. (2008). "Regulation of the activity of Escherichia coli quinolinate synthase by reversible disulfide-bond formation". Biochemistry 47 (33): 8467–8469. doi:10.1021/bi801135y. PMC 3319134. PMID 18651751.
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