title: Characterization of a thermostable short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Thermococcus sibiricus.
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.
authors.affiliation: Bach Institute of Biochemistry Russian Academy of Sciences, Leninsky pr. 33, Moscow 119071, Russia. tstekh@yandex.ru
authors.forename: Tatiana N
authors.initials: TN
authors.lastname: Stekhanova
authors.forename: Andrey V
authors.initials: AV
authors.lastname: Mardanov
authors.forename: Ekaterina Y
authors.initials: EY
authors.lastname: Bezsudnova
authors.forename: Vadim M
authors.initials: VM
authors.lastname: Gumerov
authors.forename: Nikolai V
authors.initials: NV
authors.lastname: Ravin
authors.forename: Konstantin G
authors.initials: KG
authors.lastname: Skryabin
authors.forename: Vladimir O
authors.initials: VO
authors.lastname: Popov
mesh_terms: D000426:Alcohol Dehydrogenase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D003067:Coenzymes / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D006358:Hot Temperature; D009249:NADP / Q000494:pharmacology; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D013379:Substrate Specificity; D019712:Thermococcus / Q000201:enzymology*
chemical_list: D003067:Coenzymes; D004791:Enzyme Inhibitors; D011994:Recombinant Proteins; D009249:NADP; D000426:Alcohol Dehydrogenase