Purification and Characterization of Membrane-bound Quinoprotein Cyclic Alcohol Dehydrogenase from Gluconobacter frateurii CHM 9(Microbiology & Fermentation Technology)

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概要

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• A quinoprotein catalyzing oxidation of cyclic alcohols was found in the membrane fraction for the first time, after extensive screening among aerobic bacteria. Gluconobacter frateurii CHM 9 was finally selected in this study. The enzyme tentatively named membranebound cyclic alcohol dehydrogenase (MCAD) was found to occur specifically in the membrane fraction, and pyrroloquinoline quinone (PQQ) was functional as the primary coenzyme in the enzyme activity. MCAD catalyzed only oxidation reaction of cyclic alcohols irreversibly to corresponding ketones. Unlike already known cytosolic NAD (P) H-dependent alcohol-aldehyde or alcohol-ketone oxidoreductases, MCAD was unable to catalyze the reverse reaction of cyclic ketones or aldehydes to cyclic alcohols. MCAD was solubilized and purified from the membrane fraction of the organism to homogeneity. Differential solubilization to eliminate the predominant quinoprotein alcohol dehydrogenase (ADH), and the subsequent two steps of column chromatographies, brought MCAD to homogeneity. Purified MCAD had a molecular mass of 83 kDa by SDS-PAGE. Substrate specificity showed that MCAD was an enzyme oxidizing a wide variety of cyclic alcohols. Some minor enzyme activity was found with aliphatic secondary alcohols and sugar alcohols, but not primary alcohols, differentiating MCAD from quinoprotein ADH. NAD-dependent cytosolic cyclic alcohol dehydrogenase (CCAD) in the same organism was crystallized and its catalytic and physicochemical properties were characterized. Judging from the catalytic properties of CCAD, it was apparent that CCAD was distinct from MCAD in many respects and seemed to make no contributions to cyclic alcohol oxidation.

• 2001-12-23

著者

• 足立 収生

  山口大学農学部生物機能科学科

• Moonmangmee Duangtip

  山口大農応用生物化学

• Theeragool G.

  カセサート大学理

• MOONMANGMEE Duangtip

  Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University

• FUJII Yoshikazu

  Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University

• TOYAMA Hirohide

  Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University

• THEERAGOOL Gunjana

  Department of Microbiology, Faculty of Science, Kasetsart University

• LOTONG Napha

  Department of Microbiology, Faculty of Science, Kasetsart University

• MATSUSHITA Kazunobu

  Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University

• ADACHI Osao

  Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University

• Toyama Hirohide

  Department Of Biological Chemistry Faculty Of Agriculture Yamaguchi University

• Adachi Osao

  Derartment Of Blological Chemistry Faculty Of Agriculture Yamaguchi University

• Adachi Osao

  Department Of Agricultural Chemistry Yamaguchi University

• Lotong Napha

  Department Of Microbiology Faculty Of Science Kasetsart University

• Lotong Napha

  カセサート大理 微生物

• Fujii Y

  Ritsumeikan Univ. Shiga Jpn

• Fujii Yoshikazu

  Department Of Biological Chemistry Faculty Of Agriculture Yamaguchi University

• Theeragool G.

  カセサート大理微生物

• Theeragool Gunjana

  カセサート大理 微生物

• Matsushita Kazunobu

  Department Of Biological Chemistry Faculty Of Agriculture Yamaguchi University

• Moonmangmee Duangtip

  Department Of Microbiology Faculty Of Science King Mongkut's University Of Technology Thonburi

• Moonmangmee Duangtip

  山口大農 生物機能科学

• 足立 収生

  山口大学 農

• 足立 収生

  山口大・農化

• Matsushita K

  Department Of Biological Chemistry Faculty Of Agriculture Yamaguchi University

• Theeragool Gunjana

  Department Of Microbiology Faculty Of Science Kasetsart University

• Lotong Napha

  Department Of Microbioloby Faculty Of Science Kasetsart University

• Matsushita Kazunobu

  Department of Agricultural Chemistry, Faculty of Agriculture, Yamaguchi University

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