EC Number   |
Cofactor |
Reference |
|---|
    1.1.1.47 | FAD |
the catalytic alpha-subunit contains a FAD binding motif at the N-terminal region |
654857 |
| 1.1.1.47 | more |
dual cofactor specificity due to presence of Asn215, His217, and the GXGXXA motif |
656156 |
| 1.1.1.47 | NAD+ |
- |
285784, 639095, 639097, 639103, 639105, 639106, 639107, 639108, 639109, 639110, 639111, 639115, 639118, 639120, 639123, 639124, 639126, 639127, 639128, 654301, 654857, 656156, 656567, 667087, 668130, 668349, 669452, 677305, 677657, 679607, 679608, 679611, 679613, 679615, 680592, 739842, 739861, 740382, 740388, 740529, 740857 |
| 1.1.1.47 | NAD+ |
although they can utilize both NAD+ and NADP+: GlcDH-III and GlcDH-IV prefer NAD+, and GlcDH-I and GlcDH-II prefer NADP+ |
639101 |
| 1.1.1.47 | NAD+ |
catalytic efficiency for the reaction with beta-D-glucose and NADP+ (kcat/Km) is 7.8 fold higher compared to catalytic efficiency for the reaction with beta-D-glucose and NAD+ |
718811 |
| 1.1.1.47 | NAD+ |
completely inactive with NAD+ |
639117 |
| 1.1.1.47 | NAD+ |
kcat/Km of glucose in reaction with NAD+ is about 8fold lower compared to kcat/Km of glucose in the reaction with NADP+ |
718811 |
| 1.1.1.47 | NAD+ |
NAD+ is more effective as cofactor than NADP+ on all substrates tested |
639121 |
| 1.1.1.47 | NAD+ |
the enzyme is specific for NADP+ and completely inactive with NAD+ |
285782 |
| 1.1.1.47 | NAD+ |
the enzyme prefers NAD+ rather than NADP+ |
763151 |
