Properties of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix K1

A NAD +-dependent medium-chain alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix K1 was expressed in Escherichia coli and purified. The recombinant enzyme was a homotetramer of molecular mass 1.6×10 2 kDa. The optimum pH for the oxidative reaction was around 10.5 and that fo...

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Veröffentlicht in:	Journal of Bioscience and Bioengineering 2004, Vol.97 (3), p.202-206
Hauptverfasser:	Hirakawa, Hidehiko, Kamiya, Noriho, Kawarabayashi, Yutaka, Nagamune, Teruyuki
Format:	Artikel
Sprache:	eng
Schlagworte:	Aeropyrum pernix ALCOHOL DEHYDROGENASE Archaea BACTERIA enantioselectivity medium-chain thermophilic THERMOPHILIC MICROORGANISMS thermostable
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