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
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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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Reaction
Reaction on EC 2.5.1.72 - quinolinate synthase
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glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate
model of the catalytic state. Elimination of phosphate from dihydroxyacetone phosphate may precede the condensation reaction
glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate
reaction mechanism with an early release of phosphate from dihydroxyacetone phosphate, that only, not glycerol 3-phosphate, can condense with iminoaspartate to form quinolinate. The NadA three-dimensional structure shows that there is no room in the active site to accommodate a condensation product on which the phosphate group from dihydroxyacetone phosphate is still present, overview. The enzyme has a triose phosphate isomerase activity catalyzing the reversible isomerization of glycerol 3-phosphate into dihydroxyacetone phosphate in an Fe/S-dependent manner
glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate
reaction mechanism with an early release of phosphate from dihydroxyacetone phosphate, that only, not glycerol 3-phosphate, can condense with iminoaspartate to form quinolinate. The NadA three-dimensional structure shows that there is no room in the active site to accommodate a condensation product on which the phosphate group from dihydroxyacetone phosphate is still present, overview. The enzyme has a triose phosphate isomerase activity catalyzing the reversible isomerization of glycerol 3-phosphate into dihydroxyacetone phosphate in an Fe/S-dependent manner
glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate
the presence of the Fe4S4 cluster generates an internal tunnel and a cavity to bind the substrate and and dehydrate it, which is initiated by the conserved residue Tyr21. Tyr21 is close to a conserved Thr-His-Glu. All of these residues are essential for activity and Tyr21 deprotonation, to form the reactive nucleophilic phenoxide anion, is mediated by the triad. NadA displays a dehydration mechanism significantly different from the one found in archetypical dehydratases such as aconitase, which use a serine residue deprotonated by an oxyanion hole
glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate
the presence of the Fe4S4 cluster generates an internal tunnel and a cavity to bind the substrate and and dehydrate it, which is initiated by the conserved residue Tyr21. Tyr21 is close to a conserved Thr-His-Glu. All of these residues are essential for activity and Tyr21 deprotonation, to form the reactive nucleophilic phenoxide anion, is mediated by the triad. NadA displays a dehydration mechanism significantly different from the one found in archetypical dehydratases such as aconitase, which use a serine residue deprotonated by an oxyanion hole
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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