FEBS Letters | |
Subcellular localization of vanillyl‐alcohol oxidase in Penicillium simplicissimum | |
van Berkel, Willem J.H1  Sjollema, Klaas A2  Fraaije, Marco W1  Veenhuis, Marten2  | |
[1] Department of Biomolecular Sciences, Laboratory of Biochemistry, Wageningen Agricultural University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands;Laboratory for Electron Microscopy, Biological Centre, University of Groningen, Kerklaan 30, 9750 AA Haren, The Netherlands | |
关键词: Vanillyl-alcohol oxidase; Covalent flavoprotein; Catalase-peroxidase; Peroxisome; Penicillium simplicissimum; Immunocytochemistry; | |
DOI : 10.1016/S0014-5793(97)01605-0 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
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