Crystallization (Comment) | Organism |
---|---|
hanging drop vapor diffusion technique, determination of the three-dimensional structure of the D177N mutant enzyme by X-ray cryocrystallography in the presence of NAD+ and in the presence of glucose 6-phosphate plus NADPH. The structure of a glucose 6-phosphate complex of a mutant (Q365C) with normal enzyme activity is also determined and substrate binding compared | Leuconostoc mesenteroides |
Protein Variants | Comment | Organism |
---|---|---|
D177N | absence of a negatively charged aspartate at 177 accounts for the decrease in catalytic activity at pH 7.8 | Leuconostoc mesenteroides |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
54000 | - |
2 * 54000 | Leuconostoc mesenteroides |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Leuconostoc mesenteroides | P11411 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Leuconostoc mesenteroides |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 54000 | Leuconostoc mesenteroides |
Synonyms | Comment | Organism |
---|---|---|
G6PD | - |
Leuconostoc mesenteroides |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
log-log plots of the dependence of kcat and kcat/Km on pH for both D177N and wild-type enzyme. The kcat profile for mutant enzyme D177N shows a nearly linear increase from pH 5 until wild-type-like activity is regained at pH 10. Above pH 10 the kcat decreases precipitously. Linear regression of the data in the pH range 5-10 produces a slope of 0.9 | Leuconostoc mesenteroides |