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1: FEBS Lett. 1998 Jan 23;422(1):65-8.Click here to read Links

Subcellular localization of vanillyl-alcohol oxidase in Penicillium simplicissimum.

Fraaije MW, Sjollema KA, Veenhuis M, van Berkel WJ.

Department of Biomolecular Sciences, Laboratory of Biochemistry, Wageningen Agricultural University, The Netherlands.

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 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.

PMID: 9475171 [PubMed - indexed for MEDLINE]