Subcellular localization of vanillyl-alcohol oxidase inPenicillium simplicissimum
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چکیده
منابع مشابه
Subcellular localization of vanillyl-alcohol oxidase in Penicillium simplicissimum.
Growth of Penicillium simplicissimum on anisyl alcohol, veratryl alcohol or 4-(methoxymethyl)phenol, is associated with the synthesis of relatively large amounts of the hydrogen peroxide producing flavoprotein vanillyl-alcohol oxidase (VAO). Immunocytochemistry revealed that the enzyme has a dual location namely in peroxisomes and in the cytosol. The C-terminus of the primary structure of VAO d...
متن کاملCrystallization 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...
متن کاملEnigmatic 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...
متن کاملMercuration 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...
متن کاملInversion of stereospecificity of vanillyl-alcohol oxidase.
Vanillyl-alcohol oxidase (VAO) is the prototype of a newly recognized family of structurally related oxidoreductases sharing a conserved FAD-binding domain. The active site of VAO is formed by a cavity where the enzyme is able to catalyze many reactions with phenolic substrates. Among these reactions is the stereospecific hydroxylation of 4-ethylphenol-forming (R)-1-(4'-hydroxyphenyl)ethanol. D...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1998
ISSN: 0014-5793
DOI: 10.1016/s0014-5793(97)01605-0