EC Number   |
Cofactor |
Reference |
|---|
  1.2.1.92 | more |
VvAHGD oxidizes L-AHG using both NADP+ and NAD+ as the cofactor, but VvAHGD prefers NADP+ showing an activity 3.6fold higher compared to NAD+ |
763364 |
| 1.2.1.92 | NAD+ |
- |
763364 |
| 1.2.1.92 | NAD+ |
among the cofactors, NADP+, NAD+ and NADPH, the highest abundances of reaction products are observed when NADP+ is added to the crude enzyme reaction mixture |
729648 |
| 1.2.1.92 | NAD+ |
the enzyme prefers NADP+, showing an activity 3.6fold higher than that with NAD+ |
763364 |
| 1.2.1.92 | NADP+ |
among the cofactors, NADP+, NAD+ and NADPH, the highest abundances of reaction products are observed when NADP+ is added to the crude enzyme reaction mixture |
729648 |
| 1.2.1.92 | NADP+ |
dependent on |
762876, 763358 |
| 1.2.1.92 | NADP+ |
NADP+-binding mode in enzyme VvAHGD, overview. One molecule of NADP+ is bound in the active site of each monomer, occupying the cofactor channel. The substrate channel is on the opposite side of the cofactor channel. The catalytic residues Cys282 and Glu248 are located at the junction of these two channels. These two channels are disconnected in the apo structure of VvAHGD, but connected in the structure of the VvAHGD-NADP complex. The cofactor channel has a wide opening on the protein surface, which is mostly positively charged to hold the adenosine monophosphate (AMP) moiety and the diphosphate group of NADP+. The internal part of this channel is negatively charged to accommodate the nicotinamide riboside moiety of NADP+. In the complex, the cofactor NADP+ adopts an extended conformation, which is typical for oxidized NADP+. The VvAHGD-NADP complex, NADP+ is stabilized mainly by hydrogen bond interactions |
763364 |
| 1.2.1.92 | NADP+ |
the enzyme prefers NADP+, showing an activity 3.6fold higher than that with NAD+ |
763364 |
