Properties of an Alcohol Dehydrogenase from the Hyperthermophilic Archaeon Aeropyrum pernix K1 (ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
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概要
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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 for the reductive reaction was around 8.0. The enzyme had a broad substrate specificity including aliphatic and aromatic alcohols, aliphatic and aromatic ketones, and benzylaldehyde. This enzyme produced (S)-alcohols from the corresponding ketones. The enzyme was thermophilic and the catalytic activity increased up to 95℃. It maintained 24% of the original catalytic activity after incubation for 30 min at 98℃, indicating that this enzyme is highly thermostable.
- 社団法人日本生物工学会の論文
- 2004-03-25
著者
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Nagamune Teruyuki
Department of Bioengineering, Graduate School of Engineering, The University of Tokyo
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Nagamune T
Univ. Tokyo Tokyo Jpn
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Nagamune T
Department Of Chemistry And Biotechnology School Of Engineering The University Of Tokyo
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Nagamune Teruyuki
Dep. Of Chemistry And Biotechnology Graduate School Of Engineering The Univ. Of Tokyo 7-3-1 Hongo Bu
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Nagamune Teruyuki
Department Of Bioengineering Graduate School Of Engineering The University Of Tokyo:department Of Ch
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Nagamune Teruyuki
Department Of Bioengineering Center For Nanobio Integration The University Of Tokyo:department Of Ch
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Kamiya Noriho
Department of Applied Chemistry, Graduate School of Engineering, Kyushu University
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Kamiya Noriho
Department Of Applied Chemistry Graduate School Of Engineering Kyushu University
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Kamiya Noriho
Department Of Applied Chemistry Faculty Of Engineering Kyushu University
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HIRAKAWA HIDEHIKO
Department of Chemistry and Biotechnology, School of Engineering, The University of Tokyo
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KAWARABAYASHI YUTAKA
Research Center for Glycoscience National Institute of Advancd Industrial Science and Technology
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Nagamune Teruyuki
Department Of Chemistry And Biotechnology Graduate School Of Engineering The University Of Tokyo:dep
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Hirakawa Hidehiko
Department Of Chemistry And Biotechnology School Of Engineering The University Of Tokyo
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