Molecular characterization of the recombinant iron-containing alcohol dehydrogenase from the hyperthermophilic Archaeon, Thermococcus strain ES1

Extremophiles ◽  
2008 ◽  
Vol 13 (2) ◽  
pp. 299-311 ◽  
Author(s):  
Xiangxian Ying ◽  
Amy M. Grunden ◽  
Lin Nie ◽  
Michael W. W. Adams ◽  
Kesen Ma
Keyword(s):  
Alcohol Dehydrogenase ◽  
Molecular Characterization ◽  
Hyperthermophilic Archaeon

scholarly journals Genetic and biochemical characterization of a short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosu s

2001 ◽  
Vol 268 (10) ◽  
pp. 3062-3068 ◽  
Author(s):  
John van der Oost ◽  
Wilfried G. B. Voorhorst ◽  
Servé W. M. Kengen ◽  
Ans C. M. Geerling ◽  
Vincent Wittenhorst ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Biochemical Characterization ◽  
Short Chain ◽  
Chain Alcohol ◽  
Hyperthermophilic Archaeon ◽  
Short Chain Alcohol

Purification and molecular characterization of a quinoprotein alcohol dehydrogenase from Pseudogluconobacter saccharoketogenes IFO 14464

2001 ◽  
Vol 92 (6) ◽  
pp. 524-531 ◽  
Author(s):  
Takashi Shibata ◽  
Yoshinori Ishii ◽  
Yuji Noguchi ◽  
Hisashi Yamada ◽  
Yoshimasa Saito ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Molecular Characterization

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

2010 ◽  
Vol 76 (12) ◽  
pp. 4096-4098 ◽  
Author(s):  
Tatiana N. Stekhanova ◽  
Andrey V. Mardanov ◽  
Ekaterina Y. Bezsudnova ◽  
Vadim M. Gumerov ◽  
Nikolai V. Ravin ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Alcohol Dehydrogenase ◽  
Substrate Specificity ◽  
Organic Solvents ◽  
Short Chain ◽  
Chain Alcohol ◽  
Hyperthermophilic Archaeon ◽  
Broad Substrate Specificity ◽  
Short Chain Alcohol

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.

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