Enzymatic properties of terephthalate l,2-dioxygenase of Comamonas sp. strain E6

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  • FUKUHARA Yuki
    Department of Bioengineering, Nagaoka University of Technology
  • KASAI Daisuke
    Department of Bioengineering, Nagaoka University of Technology
  • KATAYAMA Yoshihiro
    Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology
  • FUKUDA Masao
    Department of Bioengineering, Nagaoka University of Technology
  • MASAI Eiji
    Department of Bioengineering, Nagaoka University of Technology

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タイトル別名
  • Enzymatic Properties of Terephthalate 1,2-Dioxygenase of Comamonas sp. Strain E6
  • Enzymatic Properties of Terephthalate 1,2-Dioxygenase of<i>Comamonas</i>sp. Strain E6

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The tphA1II and tphA2IIA3II genes of Comamonas sp. E6 perhaps code for the terephthalate (TPA) 1,2-dioxygenase (TPADO). To characterize E6 TPADO, these genes were expressed in a His-tagged form in Escherichia coli, and the recombinant proteins were purified. TPADO activity was reconstituted from TphA1II and TphA2IIA3II, indicating that TPADO consists of a reductase (TphA1II) and a terminal oxygenase component (TphA2II and TphA3II). TphA1II contains FAD, and the presence of a plant-type [2Fe-2S] cluster was suggested. These results indicate that TPADO is a class IB aromatic ring-hydroxylating dioxygenase. NADH and NADPH were effective as electron donors for TphA1II, but NADPH appeared to be the physiological electron donor, based on the kinetic parameters. TPADO showed activity only toward TPA, and Fe2+ was required for it. The Km values for TPA and the Vmax were determined to be 72±6 μM and 9.87±0.06 U/mg respectively.

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