EC Number   |
Protein Variants |
Reference |
|---|
    5.1.3.4 | D120N |
3000fold decrease in the value of turnover number. The structure is indistinguishable from that of the wild-type enzyme and the decrease in activity is not simply due to a strutural perturbation of active site. The ratio of turnover number to Km-value is 20750fold lower than that of the wild-type enzyme |
650038 |
| 5.1.3.4 | D76E |
the ratio of turnover number to Km-value is 104fold lower than that of the wild-type enzyme,2.2fold decrease in backgroud aldolase activity compared to wild-type enzyme |
650038 |
| 5.1.3.4 | D76N |
site-directed mutants in which the putative metal ion ligand is modified: H95N, H97N, D76N. The mutant enzymes require exogenous metal ions for full activity. Their turnover numbers are greatly reduced whereas the Km-values are only moderately affected. Low levels of aldolase activity are observed with the H97N mutant, but not with D76N or the H95N mutants. The H97N mutant enzyme catalyzes the condensation of dihydroxyacetone and glycolaldehyde phosphate to produce a mixture of L-ribulose 5-phosphate and D-xylulose 5-phosphate |
2396 |
| 5.1.3.4 | D76N |
the ratio of turnover number to Km-value is 348fold lower than that of the wild-type enzyme |
2396 |
| 5.1.3.4 | E142Q |
the ratio of turnover number to Km-value is 17fold lower than that of the wild-type enzyme |
650038 |
| 5.1.3.4 | H218N |
15fold decrease in background aldolase activity compared to wild-type enzyme. The ratio of turnover number to Km-value is 296fold lower than that of the wild-type enzyme |
650038 |
| 5.1.3.4 | H59N |
site-directed mutants in which the putative metal ion ligand is modified: H95N, H97N, D76N. The mutant enzymes require exogenous metal ions for full activity. Their turnover numbers are greatly reduced whereas the Km-values are only moderately affected. Low levels of aldolase activity are observed with the H97N mutant, but not with D76N or the H95N mutants. The H97N mutant enzyme catalyzes the condensation of dihydroxyacetone and glycolaldehyde phosphate to produce a mixture of L-ribulose 5-phosphate and D-xylulose 5-phosphate |
2396 |
| 5.1.3.4 | H95N |
the ratio of turnover number to Km-value is 24.1fold lower than that of the wild-type enzyme when activated with ZnCl2 |
649983 |
| 5.1.3.4 | H95N |
the ratio of turnover number to Km-value is 676fold lower than that of the wild-type enzyme |
2396 |
| 5.1.3.4 | H97N |
13C isotope effects at pH 7 are 3.25% at C-3 and 2.69% at C4, compared to 1.85% and 1.5% for the wild-type enzyme |
649982 |
