Effect of Amino Acid Substitutions at the Active Center on the Activity of Bacillus stearothermophilus Alcohol Dehydrogenase
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概要
- 論文の詳細を見る
Catalysis of the thermostable alcohol dehydrogenase from Bacillus stearothermophilus is performed by a proton releases system involving a zinc-bound water molecule, a hydroxyl group of Thr40 (threonine position at 40), and an imidazole ring of His43. Amino acid resldues (Thr40 and His43) at the active center were substituted by Ser and Arg, respectively. Thr40Ser had a tendency toward lower activity for primary alcohols than the wild type enzyme. However, the mutant enzyme became more active for substrates with a larger side chain, such as 2-methyl-1-propanol and cyclohexanol. This phenomena might be explained by the fact that the methyl gruop of Thr40 was eliminated in Ser. His43Arg exhibited higher activity to primary alcohols (except 2-mathyl-1-propanol) and acetaldehyde (as a reverse reaction) than the wild type, but little activity for secondary alcohols and ketones. The K_m value for ethanol (K_m-e) of His43Arg was fifty-fold larger than that of the wild type. The characteristics of these mutant enzymes are also discussed.
- 公益社団法人日本生物工学会の論文
- 1992-05-25
著者
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SAKODA HISAO
Department of Biotechnology, Faculty of Engineering, Osaka University
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Imanaka Tadayuki
Department Of Applied Biotechnology Faculty Of Engineering Osaka University
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佐古田 久雄
阪大・工・応生
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Sakoda H
Osaka Univ. Osaka Jpn
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Sakoda Hisao
Department Of Biotechnology Faculty Of Engineering Osaka University
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Imanaka Tadayuki
Department Of Biotechnology Faculty Of Engineering Osaka University
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