EC Number   |
Activating Compound |
Reference |
|---|
   1.2.1.90 | ADP |
- |
727825 |
| 1.2.1.90 | ADP |
in contrast to other members of the ALDH superfamily, the enzyme from Thermoproteus tenax is regulated by a number of intermediates and metabolites. In the NAD+-dependent oxidation of D-glyceraldehyde 3-phosphate, D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP increase the affinity for the cosubstrate. In the NADP+-dependent reaction the presence of activators increases Vmax by a factor of 3. The crystal structure of the enzyme with the activating molecules reveal a common regulatory site able to accommodate the different activators |
728132 |
| 1.2.1.90 | AMP |
- |
727825 |
| 1.2.1.90 | AMP |
in contrast to other members of the ALDH superfamily, the enzyme from Thermoproteus tenax is regulated by a number of intermediates and metabolites. In the NAD+-dependent oxidation of D-glyceraldehyde 3-phosphate, D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP increase the affinity for the cosubstrate. In the NADP+-dependent reaction the presence of activators increases Vmax by a factor of 3. The crystal structure of the enzyme with the activating molecules reveal a common regulatory site able to accommodate the different activators |
728132 |
| 1.2.1.90 | D-Fructose 1-phosphate |
- |
727825 |
| 1.2.1.90 | D-fructose 6-phosphate |
- |
727825 |
| 1.2.1.90 | D-fructose 6-phosphate |
in contrast to other members of the ALDH superfamily, the enzyme from Thermoproteus tenax is regulated by a number of intermediates and metabolites. In the NAD+-dependent oxidation of D-glyceraldehyde 3-phosphate, D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP increase the affinity for the cosubstrate. In the NADP+-dependent reaction the presence of activators increases Vmax by a factor of 3. The crystal structure of the enzyme with the activating molecules reveal a common regulatory site able to accommodate the different activators |
728132 |
| 1.2.1.90 | D-glucose 1-phosphate |
- |
727825 |
| 1.2.1.90 | D-glucose 1-phosphate |
in contrast to other members of the ALDH superfamily, the enzyme from Thermoproteus tenax is regulated by a number of intermediates and metabolites. In the NAD+-dependent oxidation of D-glyceraldehyde 3-phosphate, D-glucose 1-phosphate, D-fructose 6-phosphate, AMP and ADP increase the affinity for the cosubstrate. In the NADP+-dependent reaction the presence of activators increases Vmax by a factor of 3. The crystal structure of the enzyme with the activating molecules reveal a common regulatory site able to accommodate the different activators |
728132 |
| 1.2.1.90 | D-glucose 6-phosphate |
- |
727825 |
