EC Number   |
Cofactor |
Reference |
|---|
    1.2.1.12 | 3-acetylpyridine hypoxanthine nucleotide |
1.3% of the activity with NAD+ |
287978 |
| 1.2.1.12 | 3-acetylpyridine hypoxanthine nucleotide |
3.2% of activity with NAD+ |
287978 |
| 1.2.1.12 | 3-acetylpyridine-NAD+ |
- |
287937 |
| 1.2.1.12 | 3-acetylpyridine-NAD+ |
2.8% of the activity with NAD+ |
287978 |
| 1.2.1.12 | 3-acetylpyridine-NAD+ |
4.5% of activity with NAD+ as cofactor |
287978 |
| 1.2.1.12 | C6-(4-(2,2,6,6-tetramethyl-piperidinyl-1-oxyl))-NAD+ |
can replace NAD+ as cofactor |
287942 |
| 1.2.1.12 | C8-(4-(2,2,6,6-tetramethyl-piperidinyl-l-oxyl)-amino)-NAD+ |
can replace NAD+ as cofactor |
287942 |
| 1.2.1.12 | more |
no activity with NADP+ |
741758 |
| 1.2.1.12 | more |
no activity with NADP+ or NADPH |
726190 |
| 1.2.1.12 | more |
the wild-type enzyme shows no activity with NADP+. The carboxylate group of Asp35 forms a network of hydrogen bonds with the 2' and 3-hydroxylgroups of the adenosine ribose ring of NAD+. This seems to be a critical factor to discriminate against the 2'-phosphate group of NADP+, because of electrostatic repulsion between the carboxylate group and phosphate group. Mutation of residues D35, L36, T37, and P192 alters the enzyme's cofactor specificity. Molecular docking and modelling |
743222 |
