4-hydroxy-2-methoxybenzyl alcohol oxidase
Although vanillyl alcohol (C06317) is annotated as a substrate, 4-(methoxymethyl)phenol seems to be a major substrate, according to the literature. This enzyme seems to catalyze oxidative demethylation of 4-(methoxymethyl)phenol. According to the literature [10], this enzyme catalyzes the following reactions: (A) Hydride transfer from methyl group of substrate to FAD, forming p-quinone methide intermediate and FADH2: (B) Hydride transfer from FADH2 to O2 (Re-oxidation of FAD by O2, releasing H2O2): (C) Additive double-bond deformation; Addition of H2O to p-quinone methide intermediate (Hydroxylation): (D) Eliminative double-bond formation; Elimination of H2O (or Elimination of methanol in the case of 4-(methoxymethyl)phenol as a substrate):
Vanillyl-alcohol Oxidase; Chain A, domain 4
Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2
Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3
Vanillyl-alcohol Oxidase; Chain A, domain 3
Purification and characterization of vanillyl-alcohol oxidase from Penicillium simplicissimum. A novel aromatic alcohol oxidase containing covalently bound FAD.
Asp-170 is crucial for the redox properties of vanillyl-alcohol oxidase.
X-RAY CRYSTALLOGRAPHY OF D170S MUTANT (2.8 ANGSTROMS)
Detection of intact megaDalton protein assemblies of vanillyl-alcohol oxidase by mass spectrometry.
Flavoenzymes: diverse catalysts with recurrent features.
Tuning of the product spectrum of vanillyl-alcohol oxidase by medium engineering.
Cofactor-dependent assembly of the flavoenzyme vanillyl-alcohol oxidase.
Redox properties of vanillyl-alcohol oxidase.
Laboratory-evolved vanillyl-alcohol oxidase produces natural vanillin.
Substrate specificity of flavin-dependent vanillyl-alcohol oxidase from Penicillium simplicissimum. Evidence for the production of 4-hydroxycinnamyl alcohols from 4-allylphenols.
Mercuration of vanillyl-alcohol oxidase from Penicillium simplicissimum generates inactive dimers.
Catalytic mechanism of the oxidative demethylation of 4-(methoxymethyl)phenol by vanillyl-alcohol oxidase. Evidence for formation of a p-quinone methide intermediate.
Crystallization and preliminary X-ray analysis of the flavoenzyme vanillyl-alcohol oxidase from Penicillium simplicissimum.
X-RAY CRYSTALLOGRAPHY (2.5 AND 3.2 ANGSTROMS)
Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity.
Covalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase.
X-RAY CRYSTALLOGRAPHY OF MUTANTS (2.2 ANGSTROMS)
Direction of the reactivity of vanillyl-alcohol oxidase with 4-alkylphenols.
Structural analysis of flavinylation in vanillyl-alcohol oxidase.
X-RAY CRYSTALLOGRAPHY OF MUTANTS (2.1 ANGSTROMS)
Inversion of stereospecificity of vanillyl-alcohol oxidase.
X-RAY CRYSTALLOGRAPHY OF D170S/T457E MUTANT (2.75 ANGSTROMS)