Purification and Characterization of Methanol Dehydrogenase of a Serine-Producing Methylotroph, Hyphomicrobium methylovorum
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概要
- 論文の詳細を見る
A dye-linked methanol dehydrogenase was purified to homogeneity and crystallized from a serine-producing obligate methylotroph, Hyphomicrobium methylovorum GM2. The enzyme is a dimeric protein, both subunits having a molecular mass of about 60,000 Da. Optimal activity was observed at pH 9.0 and around 35℃, the presence of NH_4 was essential for the enzyme activity. The enzyme possesses a broad substrate specificity for primary alcohols, secondary alcohols, substituted alcohols and diols and some aldehydes. The K_m value for methanol is 61 μM. The enzyme is also characterized by other detailed properties, including relatively high stability against heat treatment, no inactivation by phenazine methosulfate and no inhibition by KCN, when compared with other reported MDHs.
- 社団法人日本生物工学会の論文
- 1987-08-25
著者
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YAMADA Hideaki
Department of Agricultural Chemistry, Kyoto University
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Yamada H
Department Of Agricultural Chemistry Facutly Of Agriculture Kyoto University
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IZUMI Yoshikazu
Department of Biotechnology, Tottori University
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Yamada H
Department Of Biotechnology Faculty Of Engineering Tottori University
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Yamada H
Res. Inst. Tuberculosis Tokyo Jpn
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Yamada Hideaki
Biotechnology Research Center, Toyama Prefectural University
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MIYAZAKI SILVIA
Department of Agricultural Chemistry, Facutly of Agriculture, Kyoto University
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TOKI SHIN-ICHIRO
Department of Agricultural Chemistry, Facutly of Agriculture, Kyoto University
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Miyazaki Silvia
Department Of Agricultural Chemistry Facutly Of Agriculture Kyoto University
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Yamada H
Department Of Agricultural Chemistry Kyoto University
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Izumi Y
Tottori Univ. Tottori Jpn
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Izumi Yoshikazu
Department Of Agricultural Chemistry Kyoto University
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Toki Shin-ichiro
Department Of Agricultural Chemistry Facutly Of Agriculture Kyoto University
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Yamada Hideaki
Department Of Agricultural Chemistry Faculty Of Agriculture Kyoto University
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