Quinolinate synthase

Quinolinate synthase
Identifiers
EC number 2.5.1.72
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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 \rightleftharpoons 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. 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.
  2. 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.
  3. 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.
  4. 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.
  5. 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.

External links

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