Abstract
A new NADP(H)-dependent alcohol dehydrogenase (the YCR105W gene product, ADHVII) has been identified in Saccharomyces cerevisiae. The enzyme has been purified to homogeneity and found to be a homodimer of 40 kDa subunits and a pI of 6.2-6.4. ADHVII shows a broad substrate specificity similar to the recently characterized ADHVI (64% identity), although they show some differences in kinetic properties. ADHVI and ADHVII are the only members of the cinnamyl alcohol dehydrogenase family in yeast. Simultaneous deletion of ADH6 and ADH7 was not lethal for the yeast. Both enzymes could participate in the synthesis of fusel alcohols, ligninolysis and NADP(H) homeostasis.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alcohol Dehydrogenase / chemistry*
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Alcohol Dehydrogenase / genetics*
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Alcohol Dehydrogenase / metabolism
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Alcohol Oxidoreductases / chemistry
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Amino Acid Sequence
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Cloning, Molecular
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Dimerization
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Electrophoresis, Agar Gel
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli / metabolism
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Gene Deletion
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Hydrogen-Ion Concentration
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Kinetics
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Molecular Sequence Data
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Mutation
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NADP / metabolism
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Protein Structure, Quaternary
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Saccharomyces cerevisiae / enzymology*
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / chemistry*
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Saccharomyces cerevisiae Proteins / genetics*
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Software
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Substrate Specificity
Substances
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Saccharomyces cerevisiae Proteins
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NADP
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Alcohol Oxidoreductases
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ADH7 protein, S cerevisiae
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Alcohol Dehydrogenase
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cinnamyl alcohol dehydrogenase
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ADH6 protein, S cerevisiae