EC Number   |
General Stability |
Reference |
|---|
    1.1.1.363 | both after non-denaturing and after denaturing electrophoretic separation (SDS-PAGE) and blotting Leuconostoc mesenteroides G6PD retains its complete catalytic activity |
723154 |
| 1.1.1.363 | chymotrypsin inactivates. First order rate constant for inactivation is 0.02/min. Protection by 72 mM NAD+ or by 6.3 mM glucose 6-phosphate or 72 mM NADP+ |
721406 |
| 1.1.1.363 | eluted mutant enzyme D453C shows almost double the activity of the immobilized enzyme, which is consistent with 49% activity loss due to immobilization. Mutant enzyme D205C produces a 1.8-fold higher activity compared to its immobilized state. Eluted mutant enzyme L218C shows 9.9 times the activity of its immobilized state |
722852 |
| 1.1.1.363 | is the result of a structural change in the enzyme caused by glucose-6-phosphate dehydrogenase. In contrast to the human enzyme, the enzyme from Pseudomonas aeruginosa is not structurally stabilized by NADP+ |
760642 |
| 1.1.1.363 | pronase inactivates. First order rate constant for inactivation is 0.012/min. Protection by 72 mM NAD+ or by 6.3 mM glucose 6-phosphate or 72 mM NADP+ |
721406 |
| 1.1.1.363 | the substrate glucose-6-phosphate stabilizes the enzyme and protects it from heat and urea denaturation. The stabilization |
760642 |
| 1.1.1.363 | thermolysin inactivates. First order rate constant for inactivation is 0.057/min. Protection by 72 mM NAD+ or by 6.3 mM glucose 6-phosphate or 72 mM NADP+ |
721406 |
| 1.1.1.363 | trypsin inactivates. First order rate constant for inactivation is 0.025/min. Protection by 72 mM NAD+ or by 6.3 mM glucose 6-phosphate or 72 mM NADP+ |
721406 |
