Characterization of a thermostable short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Thermococcus sibiricus.
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.
Stekhanova
Tatiana N
TN
Bach Institute of Biochemistry Russian Academy of Sciences, Leninsky pr. 33, Moscow 119071, Russia. tstekh@yandex.ru
Mardanov
Andrey V
AV
Bezsudnova
Ekaterina Y
EY
Gumerov
Vadim M
VM
Ravin
Nikolai V
NV
Skryabin
Konstantin G
KG
Popov
Vladimir O
VO
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*
D003067:Coenzymes; D004791:Enzyme Inhibitors; D011994:Recombinant Proteins; D009249:NADP; D000426:Alcohol Dehydrogenase