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pubmed-article:9475171pubmed:abstractTextGrowth 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 displays a WKL-COOH sequence which might function as a peroxisomal targeting signal type 1 (PTS1). As VAO activity results in production of hydrogen peroxide also the subcellular location of a recently characterized co-inducible catalase-peroxidase was studied. As VAO, this hydroperoxidase is also distributed throughout the cytosol and peroxisomes.lld:pubmed
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pubmed-article:9475171pubmed:dateRevised2010-10-13lld:pubmed
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pubmed-article:9475171pubmed:articleTitleSubcellular localization of vanillyl-alcohol oxidase in Penicillium simplicissimum.lld:pubmed
pubmed-article:9475171pubmed:affiliationDepartment of Biomolecular Sciences, Laboratory of Biochemistry, Wageningen Agricultural University, The Netherlands.lld:pubmed
pubmed-article:9475171pubmed:publicationTypeJournal Articlelld:pubmed
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