Enzymatic Properties of an Extracellular Quinoprotein, Enacyloxin Oxidase
スポンサーリンク
概要
- 論文の詳細を見る
Some properties of enacyloxin (ENX) oxidase from Frateuria sp. [Oyama et al. , Biosci. Biotech. Biochem. , 58, 1914-1917 (1994)] were studied. The enzyme catalyzed the oxidation of ENX IVa, ENX IIIa, and decarbamoyl ENX IVa, specifically. The optimum pH and temperature for the enzyme activity were pH 9. 0 and 60℃, respectively. It is suggested that the enzyme is a quinoprotein but its redox cofactor is different from pyrroloquinoline quinone.
- 社団法人日本農芸化学会の論文
- 1995-01-23
著者
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WATANABE Tatsuo
School of Food and Nutritional Sciences, University of Shizuoka
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Oyama Ryo
Department Of Applied Biological Chemistry Faculty Of Agriculture Tohoku University
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IZAKI Kazuo
Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University
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WATANABE TOSHIHIKO
Department of Surgery, Tachikawa Kyosai Hospital
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SUGIYAMA Takeyoshi
Department of Agricultural Chemistry, Faculty of Agriculture, Tohoku University
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Watanabe Tatsuo
Graduate School Of Nutritional And Environmental Sciences And Coe Program In The 21st Century Univ.
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Watanabe T
Department Of Bioscience And Biotechnology Graduate School Of Agriculture Kinki University
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Watanabe Tetsuro
Department Of Bioresources Chemistry Chiba University
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杉山 長美
Tohoku Univ. Sendai Jpn
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Izaki K
Department Of Applied Biological Chemistry Faculty Of Agriculture Tohoku University
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Izaki Kazuo
Department Of Agricultural Chemistry Faculty Of Agriculture Tohoku University
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Hanzawa Hiroko
Department of Applied Biological Chemistry, Faculty of Agriculture, Tohoku University
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Sugiyama Takeyoshi
Department Of Agricultural Chemistry Faculty Of Agriculture Tohoku University
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Hanzawa Hiroko
Department Of Applied Biological Chemistry Faculty Of Agriculture Tohoku University
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Watanabe Toshihiko
Department Of Pediatric Surgery Saitama City Hospital
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Watanabe Toshihiko
Department Of Aeronautics And Astronautics University Of Tokyo
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