Enzymatic Characterization of 5-Methylthioribose 1-Phosphate Isomerase from<i>Bacillus subtilis</i>

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  • SAITO Yohtaro
    Graduate School of Biological Sciences, Nara Institute of Science and Technology (NAIST)
  • ASHIDA Hiroki
    Graduate School of Biological Sciences, Nara Institute of Science and Technology (NAIST)
  • KOJIMA Chojiro
    Graduate School of Biological Sciences, Nara Institute of Science and Technology (NAIST)
  • TAMURA Haruka
    Department of Materials Chemistry, Graduate School of Engineering, Osaka University
  • MATSUMURA Hiroyoshi
    Department of Materials Chemistry, Graduate School of Engineering, Osaka University
  • KAI Yasushi
    Department of Materials Chemistry, Graduate School of Engineering, Osaka University
  • YOKOTA Akiho
    Graduate School of Biological Sciences, Nara Institute of Science and Technology (NAIST)

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タイトル別名
  • Enzymatic Characterization of 5-Methylthioribose 1-Phosphate Isomerase from Bacillus subtilis
  • Enzymatic characterization of 5-methylthioribose 1-phosphate isomerase from <italic>Bacillus subtilis</italic>

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抄録

The product of the mtnA gene of Bacillus subtilis catalyzes the isomerization of 5-methylthioribose 1-phosphate (MTR-1-P) to 5-methylthioribulose 1-phosphate (MTRu-1-P). The catalysis of MtnA is a novel isomerization of an aldose phosphate harboring a phosphate group on the hemiacetal group. This enzyme is distributed widely among bacteria through higher eukaryotes. The isomerase reaction analyzed using the recombinant B. subtilis enzyme showed a Michaelis constant for MTR-1-P of 138 μM, and showed that the maximum velocity of the reaction was 20.4 μmol min−1 (mg protein)−1. The optimum reaction temperature and reaction pH were 35 °C and 8.1. The activation energy of the reaction was calculated to be 68.7 kJ mol−1. The enzyme, with a molecular mass of 76 kDa, was composed of two subunits. The equilibrium constant in the reversible isomerase reaction [MTRu-1-P]/[MTR-1-P] was 6. We discuss the possible reaction mechanism.

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