Characterization of a Thermostable Short-Chain Alcohol Dehydrogenase from the Hyperthermophilic Archaeon Thermococcus sibiricus | Zendy

Tatia. Stekhanova | Zendy; Andrey V. Mardanov | Zendy; Ekaterina Yu. Bezsudnova | Zendy; Vadim M. Gumerov | Zendy; Nikolai V. Ravin | Zendy; K. G. Skryabin | Zendy; Vladimir O. Popov | Zendy

Open Access

Characterization of a Thermostable Short-Chain Alcohol Dehydrogenase from the Hyperthermophilic Archaeon Thermococcus sibiricus

Author(s) -

Tatia. Stekhanova,

Andrey V. Mardanov,

Ekaterina Yu. Bezsudnova,

Vadim M. Gumerov,

Nikolai V. Ravin,

K. G. Skryabin,

Vladimir O. Popov

Publication year - 2010

Publication title -

applied and environmental microbiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.552

H-Index - 324

eISSN - 1070-6291

pISSN - 0099-2240

DOI - 10.1128/aem.02797-09

Subject(s) - thermostability , thermococcus , alcohol dehydrogenase , oxidoreductase , escherichia coli , biochemistry , enzyme , biology , alcohol , chemistry , alcohol oxidoreductase , gene , archaea , nad+ kinase

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.

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