Biology:Quinolinate synthase

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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

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 [math]\displaystyle{ \rightleftharpoons }[/math] pyridine-2,3-dicarboxylate + 2 H2O + phosphate

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

References

  1. "Quinolinate synthetase, an iron-sulfur enzyme in NAD biosynthesis". FEBS Letters 579 (17): 3737–43. July 2005. doi:10.1016/j.febslet.2005.05.065. PMID 15967443. https://hal.archives-ouvertes.fr/hal-00374522/file/NadAFEBS2.pdf. 
  2. "Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate and occur in the plastid". Plant Physiology 141 (3): 851–7. July 2006. doi:10.1104/pp.106.081091. PMID 16698895. 
  3. "Crystal structure of the NAD biosynthetic enzyme quinolinate synthase". The Journal of Biological Chemistry 280 (29): 26645–8. July 2005. doi:10.1074/jbc.C500192200. PMID 15937336. 
  4. "The [4Fe-4S] cluster of quinolinate synthase from Escherichia coli: investigation of cluster ligands". FEBS Letters 582 (19): 2937–44. August 2008. doi:10.1016/j.febslet.2008.07.032. PMID 18674537. 
  5. "Regulation of the activity of Escherichia coli quinolinate synthase by reversible disulfide-bond formation". Biochemistry 47 (33): 8467–9. August 2008. doi:10.1021/bi801135y. PMID 18651751. 

External links