EC 2.5.1.72 - Quinolinate synthase

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IntEnz Enzyme Nomenclature
EC 2.5.1.72

Names

Accepted name:
quinolinate synthase
Other names:
NadA
QS
quinolinate synthetase
Systematic name:
glycerone phosphate:iminosuccinate alkyltransferase (cyclizing)

Reaction

Cofactor

Comments:

An iron-sulfur protein that requires a [4Fe-4S] cluster for activity [1]. Quinolinate synthase catalyses the second step in the de novo biosynthesis of NAD+ from aspartate in some bacteria, with EC 1.4.3.16 (L-aspartate oxidase) catalysing the first step and EC 2.4.2.19 [nicotinate-nucleotide diphosphorylase (carboxylating)] the third step. In Escherichia coli, two of the residues that are involved in the [4Fe-4S] cluster binding appear to undergo reversible disulfide-bond formation that regulates the activity of the enzyme [5].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (246) [show] [UniProt]

References

  1. Ollagnier-de Choudens, S., Loiseau, L., Sanakis, Y., Barras, F. and Fontecave, M.
    Quinolinate synthetase, an iron-sulfur enzyme in NAD biosynthesis.
    FEBS Lett. 579: 3737-3743 (2005). [PMID: 15967443]
  2. Katoh, A., Uenohara, K., Akita, M. and Hashimoto, T.
    Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate and occur in the plastid.
    Plant Physiol. 141: 851-857 (2006). [PMID: 16698895]
  3. Sakuraba, H., Tsuge, H., Yoneda, K., Katunuma, N. and Ohshima, T.
    Crystal structure of the NAD biosynthetic enzyme quinolinate synthase.
    J. Biol. Chem. 280: 26645-26648 (2005). [PMID: 15937336]
  4. Rousset, C., Fontecave, M. and Ollagnier de Choudens, S.
    The [4Fe-4S] cluster of quinolinate synthase from Escherichia coli: investigation of cluster ligands.
    FEBS Lett. 582: 2937-2944 (2008). [PMID: 18674537]
  5. Saunders, A.H. and Booker, S.J.
    Regulation of the activity of Escherichia coli quinolinate synthase by reversible disulfide-bond formation.
    Biochemistry 47: 8467-8469 (2008). [PMID: 18651751]

[EC 2.5.1.72 created 2008]