EC Number   |
General Information |
Reference |
|---|
  1.5.3.25 | metabolism |
the active configuration of the substrate is the alpha-pyranose form. The reductive half-reaction is triphasic and is consistent either with the reaction of the substrate with the flavin followed by iminium deprotonation or hydrolysis and then product release or with the formation of flavin reduction intermediates (carbanion equivalents or adducts), followed by product release. In the oxidative half-reaction, the reduced flavin is oxidized by O2 in a single phase. The redox potentials of amadoriase at pH 7.0, 25°, show values of +48 and -52 mV for the oxidized enzyme/anionic semiquinone and anionic semiquinone/reduced enzyme couples, respectively |
764128 |
| 1.5.3.25 | metabolism |
the positive charge of Lys53 is very important for FAOX. Removal of the positive charge renders the enzyme practically dead with respect to flavin reduction. It is only the charge and not its distribution that is important |
764132 |
| 1.5.3.25 | physiological function |
conidia of the wild-type strain do not germinate on the medium containing fructosyl L-valine and NaNO2 as the sole carbon and nitrogen sources, respectively |
763944 |
| 1.5.3.25 | physiological function |
wild-type strain grows on the medium containing fructosyl L-valine as the sole carbon and nitrogen sources, a strain lacking isoform FaD-Ao2 does not. Cconidia of the wild-type strain do not germinate on the medium containing fructosyl L-valine and NaNO2 as the sole carbon and nitrogen sources, respectively |
763944 |
