Characterization In Vitro of the Hydroxylase Component of Xylene Monooxygenase, the First Enzyme of the TOL-Plasmid-Encoded Pathway for the Mineralization of Toluene and Zylenes
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概要
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The TOL plasmid from Pseudomonas putida encodes a pathway for the degradation of toluene and xylenes. The first step of this degradative pathway involves the oxidation of the methyl side chain of the substrates, which is catalyzed by xylene monooxygenase. Xylene monooxygenase consists of two components, an oxygenase component or the XylM protein, and an electron transfer component of the XylA protein. Xylane monooxygenase activity was found to be membrane-bound, and Fe^<2+> -dependent. The activity could be solubilized by two detergents, octyl-β-glucopyranoside and 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate. After separation of the solubilized enzyme by anion exchange chromatography, the stability of xylene monooxygenes was drastically reduced. As a consequence, the enzyme was characterized using the membrane vasicle fraction. The monooxygenase had a pH optimum of 7 and catalyzed the oxidation of toluene, m-xylene, p-xylene, and o-xylene, but no activity was observed towards benzyl alcohol.
- 社団法人日本生物工学会の論文
- 1995-03-25
著者
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Harayama Shigeaki
Nite Biotechnology Development Center (nbdc) National Institute Of Technology And Evaluation (nite)
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Harayama Shigeaki
Marine Biotechnology Institute Kamaishi Laboratories
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HARAYAMA Shigeaki
Department of Medical Biochemistry, University of Geneva
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SHAW JEFFREY
Department of Medical Biochemistry, Faculty of Medicine, University of Geneva
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Shaw Jeffrey
Department Of Medical Biochemistry Faculty Of Medicine University Of Geneva : (present Adress)depart
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Harayama Shigeaki
Department Of Medical Biochemistry University Medical Center
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