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The biosynthesis of methanol oxidase, a peroxisomal enzyme in the methanol-utilizing yeast Hansenula polymorpha, was studied in vitro. Translation of Hansenula mRNA in a rabbit reticulocyte lysate yields methanol oxidase protein in high amounts. The apparent molecular mass of the protein was found to be identical to the subunit of the functional multimeric enzyme, which indicates the absence of an N-terminal extension typical of most transported proteins. The regulation of methanol oxidase by glucose repression and depression as well as by induction of methanol was shown to be controlled at the level of transcription. Two mutants of Hansenula polymorpha, unable to grow on methanol as a carbon and energy source were shown to be affected in methanol oxidase synthesis.
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