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

\rightleftharpoons

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. (2005). "Quinolinate synthetase, an iron-sulfur enzyme in NAD biosynthesis". FEBS Lett. 579 (17): 3737–3743. PMID 15967443. doi:10.1016/j.febslet.2005.05.065.
↑ Katoh, A.; Uenohara, K.; Akita, M.; Hashimoto, T. (2006). "Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate and occur in the plastid". Plant Physiol. 141 (3): 851–857. PMC 1489895 . PMID 16698895. doi:10.1104/pp.106.081091.
↑ Sakuraba, H.; Tsuge, H.; Yoneda, K.; Katunuma, N.; Ohshima, T. (2005). "Crystal structure of the NAD biosynthetic enzyme quinolinate synthase". J. Biol. Chem. 280 (29): 26645–26648. PMID 15937336. doi:10.1074/jbc.C500192200.
↑ Rousset, C.; Fontecave, M.; Ollagnier de Choudens, S. (2008). "The [4Fe-4S] cluster of quinolinate synthase from Escherichia coli: Investigation of cluster ligands". FEBS Lett. 582 (19): 2937–2944. PMID 18674537. doi:10.1016/j.febslet.2008.07.032.
↑ Saunders, A.H.; Booker, S.J. (2008). "Regulation of the activity of Escherichia coli quinolinate synthase by reversible disulfide-bond formation". Biochemistry. 47 (33): 8467–8469. PMC 3319134 . PMID 18651751. doi:10.1021/bi801135y.

Quinolinate synthase at the US National Library of Medicine Medical Subject Headings (MeSH)

Transferases: alkyl and aryl (EC 2.5)
2.5.1	Dimethylallyltranstransferase Thiaminase I Methionine adenosyltransferase Riboflavin synthase Dihydropteroate synthase Spermidine synthase Glutathione S-transferase Farnesyl-diphosphate farnesyltransferase Spermine synthase Alkylglycerone phosphate synthase Farnesyltransferase Geranylgeranyltransferase type 1 Porphobilinogen deaminase

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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