Abstract
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, inorganic pyrophosphate could not be replaced by ortho- or metaphosphate. With riboflavin and ATP a slight amount of FAD formation was observed.
MeSH terms
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Adenosine Diphosphate*
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Adenosine Monophosphate*
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Adenosine Triphosphate / metabolism*
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Enzyme Stability*
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Flavin Mononucleotide*
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Flavin-Adenine Dinucleotide / biosynthesis*
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Flavin-Adenine Dinucleotide / metabolism*
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Hydrogen-Ion Concentration*
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Inorganic Pyrophosphatase / metabolism*
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Magnesium / chemistry*
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Pyrophosphatases / metabolism*
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Riboflavin / metabolism*
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Saccharomyces cerevisiae / enzymology*
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Saccharomyces cerevisiae Proteins / chemistry*
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Saccharomyces cerevisiae Proteins / isolation & purification*
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Saccharomyces cerevisiae Proteins / metabolism*
Substances
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Saccharomyces cerevisiae Proteins
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Flavin-Adenine Dinucleotide
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Adenosine Monophosphate
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Adenosine Diphosphate
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Flavin Mononucleotide
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Adenosine Triphosphate
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Pyrophosphatases
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Inorganic Pyrophosphatase
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nucleotide pyrophosphatase
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Magnesium
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Riboflavin