Purification and Properties of Methanol Dehydrogenase and Aldehyde Dehydrogenase from Methylobacillus glycogenes(Microbiology & Fermentation Industry)
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概要
- 論文の詳細を見る
Methanol dehydrogenase (MDH) and aldehyde dehydrogenase (ALDH) were purified to a homogenous state from Methylobacillus glycogenes, an obligate methylotroph. MDH (M_r 140,000) was composed of two different subunits (M_r 60,000 and 9,000) forming an α_2β_2 structure. MDH was indicated as a metalloquinoprotein containing one atom of calcium (Ca) per enzyme molecule. Binding of Ca was so tight that it was hard to remove Ca completely without denaturation of enzyme protein. A partially resolved enzyme resumed its original enzyme activity upon exogenous addition of Ca. Purified ALDH (M_r 144,000) was composed of two identical subunits of molecular mass of 72,000. ALDH was proved to be a quinoprotein in which PQQ is bound covalently.
- 社団法人日本農芸化学会の論文
著者
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Adachi Osao
Derartment Of Blological Chemistry Faculty Of Agriculture Yamaguchi University
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Adachi Osao
Laboratory Of Applied Microbiology Department Of Biological Chemistry Faculty Of Agriculture Yamaguc
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SHINAGAWA Emiko
Laboratory of Applied Microbiology, Department of Agricultural Chemistry, Faculty of Agriculture, Ya
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Ameyama M
Department Of Biological Chemistry Faculty Of Agriculture Yamaguchi University
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Ameyama Minoru
Laboratory Of Applied Microbiology Department Of Agricultural Chemistry Faculty Of Agriculture Yamag
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Shinagawa Emiko
Department Of Chemical And Biological Engineering Ube National College Of Technology
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Matsushita Kazunobu
Laboratory Of Applied Microbiology Department Of Biological Chemistry Faculty Of Agriculture Yamaguc
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