2.5.1.72: quinolinate synthase
This is an abbreviated version!
For detailed information about quinolinate synthase, go to the full flat file.
Word Map on EC 2.5.1.72
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2.5.1.72
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nada
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nicotinamide
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dihydroxyacetone
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iminoaspartate
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iron-sulfur
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pyrococcus
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dhap
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horikoshii
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qa
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cluster-containing
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oxygen-sensitive
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desulfurase
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drug development
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synthesis
- 2.5.1.72
-
nada
- nicotinamide
- dihydroxyacetone
- iminoaspartate
-
iron-sulfur
-
pyrococcus
- dhap
- horikoshii
- qa
-
cluster-containing
-
oxygen-sensitive
-
desulfurase
- drug development
- synthesis
Reaction
Synonyms
Fe4S4 quinolinate synthase, NadA, Old5, PfQS, quinolinate synthetase, SufE3, TM_1644
ECTree
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Cofactor
Cofactor on EC 2.5.1.72 - quinolinate synthase
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4Fe-4S-center
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inhibitor 4,5-dithiohydroxyphthalic acid coordinates to the enzyme [4Fe-4S] cluster through a differentiated iron site
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enzyme carries a higly oxygen-sensiteve [4Fe-4S] cluster at the NadA domain
iron-sulfur centre
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enzyme contains a [4Fe-4S]-cluster, coordinated by residues C110, C230, C320. 3.8 mol iron per mol of enzyme, 3.3 mol sulfur per mol of enzyme
iron-sulfur centre
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protein contains 3-3.5 mol iron and 3-3.5 mol sulfur per mol. Majority of the iron is in the form of a [4Fe-4S]2+ cluster. The cluster is absolutely required for activity
iron-sulfur centre
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protein contains a [4Fe-4S] cluster absolutely required for activity
iron-sulfur centre
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protein contains a [4Fe-4S] cluster absolutely required for activity
iron-sulfur centre
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protein contains a [4Fe-4S] cluster absolutely required for activity
iron-sulfur centre
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protein contains a [4Fe-4S]2+ cluster plus a small amount of a [3Fe-4S]+ cluster species. Protein contains 5 mol of iron and 2.8 mol of sulfur per mol
iron-sulfur centre
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sequence contains a Cys-W-X-Cys-Y-Z-Cys sequence characteristic for (Fe-S)4-containing proteins. Enzyme is inhibited by Fe(II)-chelating agents
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NadA contains a [4Fe-4S] cluster cofactor with a unique, non-cysteinyl-ligated, iron ion (Fea), which binds the hydroxyl group of a postulated intermediate in the last step of the reaction to facilitate a dehydration. N1 and the C7 carboxylate group of quinolinate ligate to Fea in a bidentate fashion placing the C5 hydroxyl group of the postulated final intermediate distal to Fea and virtually incapable of coordinating to it
[4Fe-4S]-center
inhibitors 4-mercaptophthalic acid, 6-mercaptopyridine-2,3-dicarboxylic acid and 5-mercaptopyrazine-2,3-dicarboxylic acid bind to the catalytic iron site of the [4Fe-4S] cluster through their thiolate
[4Fe-4S]-center
substrate dihydroxyacetone phosphate chelates the cluster