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Literature summary for 2.5.1.72 extracted from
- Crystal structure of the NAD biosynthetic enzyme quinolinate synthase (2005), J. Biol. Chem., 280, 26645-26648.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Pyrococcus horikoshii |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| in presence of substrate analogue malate. Diffraction to 2.0 A resolution. Triangular architecture composed of a 3fold repeat of three-layer alphabetaalpha sandwich folding. The active site is located at the interface of the three domains and is centered on the pseudo-3fold axis. The malate molecule is tightly held near the bottom of the active site cavity | Pyrococcus horikoshii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus horikoshii | O57767 | - |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 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 | Pyrococcus horikoshii |
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Release 2023.1 (January 2023)
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