Subcellular localization of vanillyl-alcohol oxidase in Penicillium simplicissimum

FEBS Lett. 1998 Jan 23;422(1):65-8. doi: 10.1016/s0014-5793(97)01605-0.

Abstract

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.

MeSH terms

  • Alcohol Oxidoreductases / metabolism*
  • Alcohols / metabolism
  • Cytosol / enzymology
  • Enzyme Induction / genetics
  • Flavoproteins / metabolism
  • Hydrogen Peroxide
  • Immunohistochemistry
  • Microbodies / enzymology
  • Penicillium / enzymology*
  • Peroxidases / analysis
  • Protein Sorting Signals / metabolism

Substances

  • Alcohols
  • Flavoproteins
  • Protein Sorting Signals
  • Hydrogen Peroxide
  • Alcohol Oxidoreductases
  • vanillyl-alcohol oxidase
  • Peroxidases