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Article

Assembly of alcohol oxidase in peroxisomes of the yeast Hansenula polymorpha requires the cofactor flavin adenine dinucleotide.

Molecular biology of the cell - 1 Aug 1994

Evers M E, Titorenko V I, van der Klei I J, Harder W, Veenhuis M

Abstract excerpt

The peroxisomal flavoprotein alcohol oxidase (AO) is an octamer (600 kDa) consisting of eight identical subunits, each of which contains one flavin adenine dinucleotide molecule as a cofactor. Studies on a riboflavin (Rf) auxotrophic mutant of the yeast Hansenula polymorpha revealed that limitation of the cofactor led to drastic effects on AO import and assembly as well as peroxisome proliferation. Compared to...

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Identifiers

PMID: 7803851
DOI: 10.1091/mbc.5.8.829
PMCID: PMC301104

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Assembly of alcohol oxidase in peroxisomes of the yeast Hansenula polymorpha requires the cofactor flavin adenine dinucleotide.PMID 7803851Read ↗

Flavin adenine dinucleotide binding is the crucial step in alcohol oxidase assembly in the yeast Hansenula polymorpha.Semantic proximity Read ↗

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Selective inactivation of alcohol oxidase in two peroxisome-deficient mutants of the yeast Hansenula polymorpha.Semantic proximity Read ↗

Hansenula polymorpha: an attractive model organism for molecular studies of peroxisome biogenesis and function.Semantic proximity Read ↗

Transcriptional down-regulation of peroxisome numbers affects selective peroxisome degradation in Hansenula polymorpha.Semantic proximity Read ↗

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Peroxisomes in the methylotrophic yeast Hansenula polymorpha do not necessarily derive from pre-existing organelles.Semantic proximity Read ↗

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