Subcellular localization of vanillyl‐alcohol oxidase in Penicillium simplicissimum

FEBS Letters

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