A Novel Type of D-Mannitol Dehydrogenase from Acetobacter xylinum : Occurrence, Purification, and Basic Properties
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概要
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We purified a novel type of D-mannitol dehydrogenase, which contains a c-type cytochrome and an unknown chromophore in the soluble fraction of an acetic acid bacterium, Acetobacter xylinum KU-1, to homogeneity. The enzyme showed the maximum activity at pH 5 and 40℃. It was stable up to 60℃ at pH 6, and was inhibited by Hg^<2+> and p-quinone (K_i=0.18 mM). The molecular weight of the enzyme was about 140,000, and those of the subunits were 69,000, 51,000, and 20,000; the enzyme is hetero-trimeric and contained 8 g-atoms of Fe per mole. The α-helix content was estimated to be about 52.9%. The enzyme catalyzed phenazine methosulfate dependent oxidation of D-mannitol with an apparent K_m of 98μM (for D-mannitol) and V_<max> of 213 μmol/min/mg. The reduced form of the enzyme showed the absorption maxima at 386, 416, 480, 518, 550, and 586 nm, which are attributable to a c-type cytochrome in the enzyme.
- 1997-10-23
著者
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Soda Kenji
Department Of Biotechnology Faculty Of Engineering Kansai University
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TSUKAGAWA Yasuyuki
Department of Biotechnology, Faculty of Engineering, Kansai University
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Oikawa Tadao
Department Of Biotechnology Faculty Of Engineering Kansai University
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Soda Kenji
Department Of Biotechnology Faculty Of Engineering Kansai University:kansai University High Technolo
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OKITA Tadao
Department of Biotechnology, Faculty of Engineering, Kansai University
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NAKAI Junji
Department of Biotechnology, Faculty of Engineering, Kansai University
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Nakai Junji
Department Of Biotechnology Faculty Of Engineering Kansai University
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Okita Tadao
Department Of Biotechnology Faculty Of Engineering Kansai University:kansai University High Technolo
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Soda Kenji
Department of Bioresources Chemistry, Graduate School of Natural Science and Technology, Okayama University
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