EC Number   |
General Information |
Reference |
|---|
   1.1.3.7 | evolution |
the enzyme belongs to the AA3_2 subfamily, phylogenetic analysis |
741720 |
| 1.1.3.7 | evolution |
the enzyme belongs to the glucose methanol choline oxidase superfamily |
724757 |
| 1.1.3.7 | evolution |
the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis and phylogenetic tree, overview |
724064 |
| 1.1.3.7 | evolution |
the enzyme belongs to the glucose methanol choline oxidase superfamily, structure-function analysis by mixed quantum mechanics/molecular mechanics studies, overview |
724224 |
| 1.1.3.7 | evolution |
the enzyme belongs to the glucosemethanolcholine oxidase superfamily |
724349 |
| 1.1.3.7 | metabolism |
aryl-alcohol oxidase, AAO, participates in fungal degradation of lignin, a process of high ecological and biotechnological relevance, by providing the hydrogen peroxide required by ligninolytic peroxidases, mechanism, overview |
698931 |
| 1.1.3.7 | metabolism |
temperature dependence of hydride transfer from the substrate to the N5 of the FAD cofactor during the reductive half-reaction. Kinetic isotope effects suggest an environmentally-coupled quantum-mechanical tunnelling process. AAO shows a preorganized active site that would only require the approaching of the hydride donor and acceptor for the tunnelled transfer to take place |
763550 |
| 1.1.3.7 | metabolism |
the enzyme is important in the 5-hydroxymethylfurfural degradation pathway, verview |
742493 |
| 1.1.3.7 | more |
AAO shows a buried active site connected to the solvent by a hydrophobic funnel-shaped channel, with Phe501 and two other aromatic residues forming a narrow bottleneck that prevents the direct access of alcohol substrates, while O2 has access to the active site following this channel. The side chain of Phe501, contiguous to the catalytic His502 in AAO, helps to position O2 at an adequate distance from flavin C4a (and His502Nepsilon). Phe501 substitution with a bulkier tryptophan residue results in an increase in theO2 reactivity of this flavoenzyme, free diffusion simulations of O2 inside the active-site cavity of AAO, the O2 reactivity of AAO decreases when the access channel is enlarged and increases when it is constricted by introducing a tryptophan residue, overview |
725449 |
| 1.1.3.7 | more |
docking of 4-methoxybenzyl alcohol at the buried crystal active site, and quantum mechanical/molecular mechanical study, overview |
724757 |
