Subcellular localization of vanillyl-alcohol oxidase in Penicillium simplicissimum.

Enigmatic Gratuitous Induction of the Covalent Flavoprotein Vanillyl-Alcohol Oxidase in Penicillium simplicissimum.

When Penicillium simplicissimum is grown on veratryl alcohol, anisyl alcohol, or 4-(methoxymethyl)phenol, an intracellular covalent flavin-containing vanillyl-alcohol oxidase is induced. The induction is highest (up to 5% of total protein) during the growth phase. In addition to vanillyl-alcohol oxidase, an intracellular catalase-peroxidase is induced. Induction of vanillyl-alcohol oxidase in P...

Mercuration of vanillyl-alcohol oxidase from Penicillium simplicissimum generates inactive dimers.

Vanillyl-alcohol oxidase (EC 1.1.3.7) from Penicillium simplicissimum was modified with p-mercuribenzoate. One cysteine residue reacts rapidly without loss of enzyme activity. Three sulfhydryl groups then react in an 'all or none process' involving enzyme inactivation and dissociation of the octamer into dimers. The inactivation reaction is slowed down in the presence of the competitive inhibit...

Crystallization and preliminary X-ray analysis of the flavoenzyme vanillyl-alcohol oxidase from Penicillium simplicissimum.

Vanillyl-alcohol oxidase catalyses the oxidation of several 4-hydroxybenzyl alcohols by using 8-alpha-(N3-histidyl)-FAD as a covalently bound prosthetic group. Crystals of vanillyl-alcohol oxidase from Penicillium simplicissimum have been grown by using the vapor diffusion technique. The space group was found to be I, with cell dimensions a = b = 140.5 A, c = 132.9 A. Diffraction data have been...

University of Groningen Enigmatic Gratuitous Induction of the Covalent Flavoprotein Vanillyl-Alcohol Oxidase in Penicillium simplicissimum Fraaije, Marco; Pikkemaat,

Biocatalytic Properties and Structural Analysis of Eugenol Oxidase from Rhodococcus jostii RHA1: A Versatile Oxidative Biocatalyst

Eugenol oxidase (EUGO) from Rhodococcus jostii RHA1 had previously been shown to convert only a limited set of phenolic compounds. In this study, we have explored the biocatalytic potential of this flavoprotein oxidase, resulting in a broadened substrate scope and a deeper insight into its structural properties. In addition to the oxidation of vanillyl alcohol and the hydroxylation of eugenol, ...