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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Subcellular localization of vanillyl-alcohol oxidase in Penicillium simplicissimum.

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.[1]

References

  1. Subcellular localization of vanillyl-alcohol oxidase in Penicillium simplicissimum. Fraaije, M.W., Sjollema, K.A., Veenhuis, M., van Berkel, W.J. FEBS Lett. (1998) [Pubmed]
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