Characterization of a Thermostable Short-Chain Alcohol Dehydrogenase from the Hyperthermophilic Archaeon Thermococcus sibiricus
2010 ◽
Vol 76
(12)
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pp. 4096-4098
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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.
2001 ◽
Vol 268
(10)
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pp. 3062-3068
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2001 ◽
Vol 276
(26)
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pp. 24194-24202
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2012 ◽
Vol 169
(15)
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pp. 1435-1444
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