EC Number   |
Cofactor |
Reference |
|---|
    1.1.1.363 | NAD+ |
- |
721401, 721402, 721406, 721511, 722476, 722581, 723730, 740461, 740878, 742533, 761295 |
| 1.1.1.363 | NAD+ |
can utilize either NADP+ or NAD+ as coenzyme |
721411 |
| 1.1.1.363 | NAD+ |
kcat/Km of NADP+ is 9.3fold higher compared to kcat/Km of D-glucose 6-phosphate in NAD+-dependent reaction, kcat/Km of D-glucose 6-phosphate in the NADP+-dependent reaction is 3.5fold higher compared to kcat/Km of D-glucose 6-phosphate in NAD+-dependent reaction. kcat/Km of D-glucose 6-phosphate in the NADP+-dependent reaction is 3.5fold higher compared to kcat/Km of D-glucose 6-phosphate in NAD+-dependent reaction |
723718 |
| 1.1.1.363 | NAD+ |
NAD+-reducing activity is higher than NADP+-reducing activity |
740421 |
| 1.1.1.363 | NAD+ |
the maximum quenching of protein fluorescence is 50% for NAD+. The dissociation constant for NAD+ is 2.5 mM |
721400 |
| 1.1.1.363 | NAD+ |
the mechanism with NAD+ is more complex compared to the reaction with D-glucose 6-phosphate and NADP+ |
722578 |
| 1.1.1.363 | NAD+ |
the NAD+/enzyme complex is half-open. It is suggested that if NAD+ approaches the open form of the enzyme, and this approach generates a conformation change, initially to the half-open form. The concomitant movement of the coenzyme sheet allows Gln47 to approach the adenine ribose 20-hydroxyl and moves away the side chain of Arg46 |
721145 |
| 1.1.1.363 | NAD+ |
wild-type enzyme prefers NADP+ as coenzyme |
721411 |
| 1.1.1.363 | NADH |
- |
742533 |
| 1.1.1.363 | NADP+ |
- |
721401, 721402, 721406, 721511, 722476, 722581, 723730, 740461, 740878, 761295 |
