Modification of flavin adenine dinucleotide in alcohol oxidase of the yeast Hansenula polymorpha

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

We have studied the role of flavin adenine dinucleotide (FAD) in the in vivo assembly of peroxisomal alcohol oxidase (AO) in the yeast Hansenula polymorpha. In previous studies, using a riboflavin (Rf) autotrophic mutant, an unequivocal judgement could not be made, since Rf-limitation led to a partial block of AO import in this mutant. This resulted in the accumulation of AO precursors in the c...

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Combination with Flavin Adenine Dinucleotide*

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Isolation of mutants of Hansenula polymorpha defective in the assembly of octameric alcohol oxidase.

Alcohol oxidase (AO) is a peroxisomal enzyme that catalyses the first step in methanol metabolism in yeast. Monomeric, inactive AO protein is synthesised in the cytosol and subsequently imported into peroxisomes, where the enzymatically active, homo-octameric form is found. The mechanisms involved in AO octamer assembly are largely unclear. Here we describe the isolation of Hansenula polymorpha...

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Reversible enzymatic synthesis of flavin-adenine dinucleotide.

An enzyme has been partially purified from brewer's yeast which catalyzes the reversible reaction between riboflavin phosphate and adenosine triphosphate (ATP) on the one hand and flavin-adenine dinucleotide (FAD) and inorganic pyrophosphate on the other in the presence of magnesium ions. ATP could not be replaced by adenosine diphosphate or adenosine-5-phosphate, and in the reverse reaction, i...

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ژورنال

عنوان ژورنال: Journal of General Microbiology

سال: 1991

ISSN: 0022-1287

DOI: 10.1099/00221287-137-10-2381