Abstract
An NADPH-dependent alpha-keto amide reductase was purified from Saccharomyces cerevisiae. The molecular mass of the native enzyme was estimated to be 33 and 36 kDa by gel filtration chromatography and SDS-polyacrylamide gel electrophoresis, respectively. The purified enzyme showed a reducing activity not only for aromatic alpha-keto amides but also for aliphatic and aromatic alpha-keto esters. The internal sequence of the enzyme was identical with that of a hypothetical protein (ORF YDL 124w) coded by yeast chromosome IV.
MeSH terms
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Alcohol Oxidoreductases / chemistry*
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Alcohol Oxidoreductases / isolation & purification
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Ammonium Sulfate
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Esters / chemistry
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Hydrogen-Ion Concentration
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Indicators and Reagents
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Keto Acids / chemistry
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Kinetics
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Molecular Conformation
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Molecular Weight
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Oxidation-Reduction
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Protamines
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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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Stereoisomerism
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Substrate Specificity
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Temperature
Substances
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Esters
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Indicators and Reagents
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Keto Acids
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Protamines
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Saccharomyces cerevisiae Proteins
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Alcohol Oxidoreductases
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YDL124W protein, S cerevisiae
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Ammonium Sulfate