EC Number |
Cofactor |
Reference |
---|
1.1.3.4 | FAD |
not detectable in honey enzyme |
389818 |
1.1.3.4 | FAD |
semiempirical quantum chemical calculations are used to investigate the role of FAD in the catalytic oxidation of glucose. Only the hydride ion is transferred to the FAD coenzyme |
728045 |
1.1.3.4 | FAD |
the active site holds the tightly, non-covalently bound FAD cofactor |
743277 |
1.1.3.4 | flavin |
both the thermal and chemical denaturation of the enzyme cause dissociation of the flavin cofactor |
656254 |
1.1.3.4 | Flavin-hypoxanthine dinucleotide |
FHD, can substitute FAD |
389802 |
1.1.3.4 | more |
FAD-binding site studies, active site geometry |
389827 |
1.1.3.4 | more |
specification of the relative contribution of structure and dynamics to the catalytic activity, using infrared absorption spectroscopy of the amide I' band, tryptophan fluorescence quenching and hydrogen isotopic exchange on the oxidized and reduced enzymes |
389836 |