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 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". FEBS Letters. 579 (17): 3737–43. 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. 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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