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
Quinolinate synthase | |||||||||
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Identifiers | |||||||||
EC no. | 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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This iron-sulfur protein that requires a [4Fe-4S] cluster for activity.
References
edit- ^ 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
edit- Quinolinate+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)