From Wikipedia, the free encyclopedia
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
-
^ 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.
-
^ 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.
-
^ 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.
-
^ 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.
-
^ 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.
External links
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