TY - JOUR
T1 - Properties of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix K1
AU - Hirakawa, Hidehiko
AU - Kamiya, Noriho
AU - Kawarabayashi, Yutaka
AU - Nagamune, Teruyuki
N1 - Funding Information:
We are grateful to the Department of Biotechnology, National Institute of Technology and Evaluation which kindly provided the A2GR7175 shot-gun clone containing an alcohol dehydrogenase coding sequence (ORF: APE2239). The present work was supported partly by a Grant-in-Aid for the 21st century COE program, “Human-Friendly Material Based on Chemistry” from the Ministry of Education, Culture, Sports, Science and Technology of Japan.
PY - 2004
Y1 - 2004
N2 - 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 1.6×102 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°C. It maintained 24% of the original catalytic activity after incubation for 30 min at 98°C, indicating that this enzyme is highly thermostable.
AB - 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 1.6×102 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°C. It maintained 24% of the original catalytic activity after incubation for 30 min at 98°C, indicating that this enzyme is highly thermostable.
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U2 - 10.1263/jbb.97.202
DO - 10.1263/jbb.97.202
M3 - Article
C2 - 16233615
AN - SCOPUS:1842451878
VL - 97
SP - 202
EP - 206
JO - Journal of Bioscience and Bioengineering
JF - Journal of Bioscience and Bioengineering
SN - 1389-1723
IS - 3
ER -