EC Number   |
Cofactor |
Reference |
|---|
   1.1.1.30 | more |
no activity with NADP+/NADPH |
680512 |
| 1.1.1.30 | NAD+ |
- |
286512, 286513, 286514, 286515, 286516, 286517, 286518, 286519, 286520, 286521, 286522, 286523, 286524, 286525, 286526, 286527, 286528, 286529, 286530, 286531, 286532, 286533, 286534, 286535, 286536, 286537, 286538, 286539, 286540, 286541, 286542, 286543, 655126, 655261, 656326, 668251, 668322, 669434, 669544, 669873, 679792, 680512, 685409, 689351, 695376, 711807, 721853, 729048, 737394, 737467, 739558 |
| 1.1.1.30 | NAD+ |
NAD+ is bound in a large cleft in the domain. The diphosphate group of NAD+ is covered by the small additional domain, which is supported by two extended arms allowing domain movement |
684149 |
| 1.1.1.30 | NAD+ |
the substrate-binding loop, residues 187-210, is partially disordered in several subunits, in both the presence and absence of NAD+, closed conformation in the complex structure with NAD+, interactions of Val185, Thr187 and Leu189 with the cosubstrate induced the conformational change from open to closed, NAD+ binding increases the flexibility of the substrate-binding loop and shifts the equilibrium between the open and closed forms towards the closed form |
679792 |
| 1.1.1.30 | NADH |
- |
655126, 655261, 656326, 669544, 679792, 680512, 695376, 737912, 737914 |
| 1.1.1.30 | NADP+ |
2% of the activity with NAD+ |
669873 |
