Quinolinate synthase

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
Quinolinate synthase
Identifiers
EC number2.5.1.72
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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. 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.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.