Abstract
Short-chain alcohol dehydrogenase, encoded by the gene Tsib_0319 from the hyperthermophilic archaeon Thermococcus sibiricus, was expressed in Escherichia coli, purified and characterized as an NADPH-dependent enantioselective oxidoreductase with broad substrate specificity. The enzyme exhibits extremely high thermophilicity, thermostability, and tolerance to organic solvents and salts.
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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Coenzymes / pharmacology
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Enzyme Inhibitors / pharmacology
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Enzyme Stability
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Escherichia coli / genetics
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Gene Expression
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Hot Temperature
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NADP / pharmacology
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Substrate Specificity
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Thermococcus / enzymology*
Substances
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Coenzymes
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Enzyme Inhibitors
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Recombinant Proteins
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NADP
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Alcohol Dehydrogenase