Enzyme

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     2. Transferases
        2.5 Transferring alkyl or aryl groups, other than methyl groups
            2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
ID:2.5.1.72
Description:Quinolinate synthase.
Alternative Name: Quinolinate synthetase.
Cath: 1.20.58.100; 3.50.50.60; 3.90.700.10; 3.40.50.10800;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.5.1.72
BRENDA Enzyme Link: BRENDA 2.5.1.72
KEGG Enzyme Link: KEGG2.5.1.72
BioCyc Enzyme Link: BioCyc 2.5.1.72
ExPASy Enzyme Link: ExPASy2.5.1.72
EC2PDB Enzyme Link: EC2PDB 2.5.1.72
ExplorEnz Enzyme Link: ExplorEnz 2.5.1.72
PRIAM enzyme-specific profiles Link: PRIAM 2.5.1.72
IntEnz Enzyme Link: IntEnz 2.5.1.72
MEDLINE Enzyme Link: MEDLINE 2.5.1.72
MSA:

2.5.1.72;

Phylogenetic Tree:

2.5.1.72;

Uniprot:
M-CSA:
RHEA:25888 dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
RULE(radius=1) [*:1]-[C;H0;+0:2](=[NH;+0:3])-[CH2;+0:4]-[*:5].[*:6]-[O;H0;+0:7]-[CH2;+0:8]-[C;H0;+0:9](=[O;H0;+0:10])-[CH2;+0:11]-[OH;+0:12]>>[*:6]-[OH;+0:7].[*:1]-[c;H0;+0:2]1:[n;H0;+0:3]:[cH;+0:11]:[cH;+0:9]:[cH;+0:8]:[c;H0;+0:4]:1-[*:5].[OH2;+0:12].[OH2;+0:10]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The [4Fe-4S] cluster of quinolinate synthase from Escherichia coli: investigation of cluster ligands.Rousset C, Fontecave M, Ollagnier de Choudens S2008 Aug 2018674537
Quinolinate synthetase, an iron-sulfur enzyme in NAD biosynthesis.Ollagnier-de Choudens S, Loiseau L, Sanakis Y, Barras F, Fontecave M2005 Jul 415967443
Crystal structure of the NAD biosynthetic enzyme quinolinate synthase.Sakuraba H, Tsuge H, Yoneda K, Katunuma N, Ohshima T2005 Jul 2215937336