EC Number   |
Reaction |
Reference |
|---|
   1.1.3.7 | an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2 |
- |
- |
| 1.1.3.7 | an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2 |
a sequential mechanism in which O2 reacts with reduced enzyme before release of the aldehyde product, the AAO reductive half-reaction is essentially irreversible and rate limiting during catalysis, a synchronous mechanism in which hydride transfer from substrate alpha-carbon to FAD and proton abstraction from hydroxyl occur simultaneously, reaction mechanism, overview. The AAO catalytic mechanism proceeds via electrophilic attack and direct transfer of a hydride to the flavin |
698931 |
| 1.1.3.7 | an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2 |
belongs to the GMC oxidoreductase family (GMC: glucose-methanol-choline) |
680907 |
| 1.1.3.7 | an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2 |
catalytic mechanism with catalytic cycle including two half-reactions, overview. Proton transfer to His502 acting as a base, His546 plays a role in alcohol binding. Phe501 forces O2 to approach the flavin C4a, and His502 yielding hydrogen peroxide and the reoxidized flavin |
724064 |
| 1.1.3.7 | an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2 |
kinetic and reaction mechanisms involving residue Tyr92, hydride transfer reaction and aromatic stacking interactions on catalysis. Sequential reaction mechanism involving a ternary complex between AAO and its reducing/oxidizing substrates versus a ping-pong mechanism, overview |
742493 |
| 1.1.3.7 | an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2 |
modeling protein-ligand recognition mechanisms, substrate diffusion into the AAO active site, two conserved histidine residues, His502 and His546, are involved in catalysis, structure-function analysis, overview |
724224 |
| 1.1.3.7 | an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2 |
oxidation mechanism by AAO, overview |
724757 |
| 1.1.3.7 | an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2 |
the enzyme catalyzes two half-reactions: oxidation of benzyl alcohol with FAD cofactor, and reduction of O2 with reduced cofactor FADH2, active site structure, Tyr92, Phe501, His502 and His546 are strictly required for activity, Tyr78 is not involved in catalysis, while Leu315 might be important |
673566 |
| 1.1.3.7 | an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2 |
the enzyme catalyzes two half-reactions: oxidation of benzyl alcohol with FAD cofactor, and reduction of O2 with reduced cofactor FADH2, the enzyme does not thermodynamically stabilize a flavin semiquinone radical and forms no sulphite adduct |
671834 |
| 1.1.3.7 | an aromatic primary alcohol + O2 = an aromatic aldehyde + H2O2 |
two conserved histidine residues, His502 and His546, are involved in catalysis and play roles in the two half-reactions, with a stronger histidine involvement in the reductive than in the oxidative half-reaction. His502 is the catalytic base in the AAO reductive half-reaction. The His502 proton transfer does not limit the oxidative half-reaction, stereoselective hydride transfer. Quantum mechanical/molecular mechanical study, mutational analysis, and computational simulations, detailed overview |
724349 |
