Enzymatic Characterization of 5-Methylthioribose 1-Phosphate Isomerase from Bacillus subtilis

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概要

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• 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.

• 社団法人 日本農芸化学会の論文

著者

• MATSUMURA Hiroyoshi

  Department of Materials Chemistry, Graduate School of Engineering, Osaka University

• KAI Yasushi

  Department of Materials Chemistry, Graduate School of Engineering, Osaka University

• Kojima Chojiro

  Graduate School of Biological Sciences, Nara Institute of Science and Technology

• Ashida Hiroki

  Graduate School Of Biological Sciences Nara Institute Of Science And Technology

• Yokota Akiho

  Graduate School Of Biological Sciences Nara Institute Of Science And Technology

• Saito Yohtaro

  Graduate School of Biological Sciences, Nara Institute of Science and Technology (NAIST)

• TAMURA Haruka

  Department of Materials Chemistry, Graduate School of Engineering, Osaka University

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