Vanillyl-alcohol oxidase (VAO)

Vanillyl-alcohol oxidase (VAO) is a flavoprotein oxidoreductase that primarily catalyzes the oxidation of vanillyl alcohol and a broad range of other substituted phenolic alcohols to their corresponding aldehydes, with simultaneous reduction of molecular oxygen to hydrogen peroxide[6][7][5][1]. It is a homo-octameric enzyme found in organisms such as *Penicillium simplicissimum* and belongs to the VAO/PCMH family of flavoenzymes[4][1]. VAO uses a firmly bound FAD cofactor for redox catalysis, showing a preference for para-substituted phenols and comprising a unique substrate specificity compared to other aryl alcohol oxidases[3][5][1]. The enzyme is of interest in biotechnology for the biosynthesis of vanillin and fine chemicals, but does not have a direct therapeutic application or known disease linkage in humans[1][6][7]. Its physiological substrate is presumed to be 4-(methoxymethyl)phenol, and it has been structurally characterized by several crystal structures[5][6]. VAO participates in pathways such as degradation of aromatic compounds, e.g., 2,4-dichlorobenzoate[6].

Other names

4-hydroxy-2-methoxybenzyl alcohol oxidasevanillyl alcohol:oxygen oxidoreductase

Catalyzes the oxidation of vanillyl alcohol and related compounds to their corresponding aldehydes, using FAD as a cofactor and molecular oxygen as the electron acceptor, producing hydrogen peroxide[5][6][7][1]