EC Number   |
Reaction |
Reference |
|---|
   1.1.3.9 | D-galactose + O2 = D-galacto-hexodialdose + H2O2 |
- |
- |
| 1.1.3.9 | D-galactose + O2 = D-galacto-hexodialdose + H2O2 |
detailed mechanism, selective for pro-S hydrogen abstraction |
654732 |
| 1.1.3.9 | D-galactose + O2 = D-galacto-hexodialdose + H2O2 |
detailed reaction mechanism, the active site of galactose oxidase bears a Cu2+ with an inner coordination sphere involving Tyr272, Tyr495, His496, His581, and a coordinated solvent molecule, and Trp290 in the outer sphere of the complex, overview |
671578 |
| 1.1.3.9 | D-galactose + O2 = D-galacto-hexodialdose + H2O2 |
mechanism |
656711 |
| 1.1.3.9 | D-galactose + O2 = D-galacto-hexodialdose + H2O2 |
oxidative and reductive half-reactions in the enzymatic cycle of galactose oxidase during oxidation of the C-6 hydroxyl group of D-galactose to the corresponding aldehyde |
-, 743101 |
| 1.1.3.9 | D-galactose + O2 = D-galacto-hexodialdose + H2O2 |
reaction mechanism, structure-function analysis, two-electron redox reaction involving a Cu(I)/Cu(II) couple and the reversible oxidation of a ligating phenolate, tyrosine residue of the Tyr272-Cys228 conjugate, to a phenoxyl radical, overview |
674912 |
| 1.1.3.9 | D-galactose + O2 = D-galacto-hexodialdose + H2O2 |
the active site consists of two one-electron redox units involving residues Y495, H496, H581, Y272, and W290, a Cu2+ ion, and a crosslinked Y272-C228 radical cofactor, which together are responsible for the catalytic activity, structure modelling |
674186 |
| 1.1.3.9 | D-galactose + O2 = D-galacto-hexodialdose + H2O2 |
the catalytic mechanism of enzyme GOase can be described by the ping-pong bi bi mechanism, where the alcohol substrate is oxidized in one catalytic halfreaction followed by reoxidation of the enzyme by reduction of oxygen to hydrogen peroxide in a second half-reaction |
-, 743392 |
| 1.1.3.9 | D-galactose + O2 = D-galacto-hexodialdose + H2O2 |
the first half-reaction involves proton transfer from O-6 of galactose to the axial tyrosine anion, hydrogen atom transfer (HAT) from C-6 of galactose to the tyrosine-cysteine radical cofactor and electron transfer from the carbohydrate to generate the aldehyde and Cu(I). To complete the catalytic cycle, the second half-reaction is proposed to involve inner-sphere electron transfer from Cu(I) to oxygen to yield superoxide, HAT from the phenolic hydroxyl group of the Tyr-Cys cofactor to the superoxide to produce metal-bound hydroperoxide and proton transfer from the axial tyrosine to hydroperoxide to produce hydrogen peroxide and the re-oxidized, active Cu(II)-radical state of the enzyme |
743337 |
