EC Number   |
Reaction |
Reference |
|---|
    2.5.1.72 | glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate |
- |
- |
| 2.5.1.72 | 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 |
687499 |
| 2.5.1.72 | 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 |
737716 |
| 2.5.1.72 | 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 |
-, 738452 |
