Premium
Subcellular localization of vanillyl‐alcohol oxidase in Penicillium simplicissimum
Author(s) -
Fraaije Marco W,
Sjollema Klaas A,
Veenhuis Marten,
van Berkel Willem J.H
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01605-0
Subject(s) - peroxisome , alcohol oxidase , biochemistry , oxidase test , chemistry , flavoprotein , hydrogen peroxide , cytosol , catalase , peroxidase , enzyme , peroxisomal targeting signal , gene , pichia pastoris , recombinant dna
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.