Subcellular localization of vanillyl-alcohol oxidase in Penicillium simplicissimum

被引:12
作者
Fraaije, MW
Sjollema, KA
Veenhuis, M
van Berkel, WJH
机构
[1] Agr Univ Wageningen, Biochem Lab, Dept Biomol Sci, NL-6703 HA Wageningen, Netherlands
[2] Univ Groningen, Ctr Biol, Lab Electron Microscopy, NL-9750 AA Haren, Netherlands
关键词
vanillyl-alcohol oxidase; covalent flavoprotein; catalase-peroxidase; peroxisome; Penicillium simplicissimum; immunocytochemistry;
D O I
10.1016/S0014-5793(97)01605-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Growth of Penicillium simplicissimum on anisyl alcohol, veratryl alcohol or 3-(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. (C) 1998 Federation of European Biochemical Societies.
引用
收藏
页码:65 / 68
页数:4
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