EC Number   |
Cofactor |
Reference |
|---|
   5.1.3.20 | more |
preference of the enzyme for NAD+ compared to NADP+. When NADP is bound, the binding region assumes a different conformation |
727070 |
| 5.1.3.20 | NAD+ |
AGME preferentially utilizes NADP+ but can use NAD+ (lower activity) |
716848 |
| 5.1.3.20 | NAD+ |
can substitute for NADP+, Kd: 0.045 mM |
652147 |
| 5.1.3.20 | NAD+ |
contains 1 mol of tightly bound NAD+ per mol of enzyme subunit |
2357 |
| 5.1.3.20 | NAD+ |
preferred cofactor compared to NADP+, binds at the enzyme active site, binding site structure, overview |
727070 |
| 5.1.3.20 | NADP+ |
a large N-terminal domain consists of a modified seven-stranded Rossmann fold that is associated with NADP+ binding |
653940 |
| 5.1.3.20 | NADP+ |
AGME preferentially utilizes NADP+ |
716848 |
| 5.1.3.20 | NADP+ |
bound to the enzyme, involved in catalysis |
661199 |
| 5.1.3.20 | NADP+ |
evidence for a direct oxidation mechanism in which the hydride initially transferred to the NADP+ cofactor is subsequently returned to the same carbon in a nonstereospecific manner |
663007 |
| 5.1.3.20 | NADP+ |
NAD+ is the preferred cofactor |
727070 |
