Biology:Quinolinate synthase
From HandWiki
Quinolinate synthase | |||||||||
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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 | ||||||||
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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
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ "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.
- ↑ "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
- Quinolinate+synthase at the US National Library of Medicine Medical Subject Headings (MeSH)
Original source: https://en.wikipedia.org/wiki/Quinolinate synthase.
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