Applied Microbiology and Biotechnology

, Volume 73, Issue 1, pp 95–102

Regioselective carboxylation of 1,3-dihydroxybenzene by 2,6-dihydroxybenzoate decarboxylase of Pandoraea sp. 12B-2


  • Tsuyoshi Matsui
    • Department of Biomolecular ScienceGifu University
  • Toyokazu Yoshida
    • Department of Biomolecular ScienceGifu University
  • Tomohiro Yoshimura
    • Department of Biomolecular ScienceGifu University
    • Department of Biomolecular ScienceGifu University
Biotechnologically Relevant Enzymes and Proteins

DOI: 10.1007/s00253-006-0437-z

Cite this article as:
Matsui, T., Yoshida, T., Yoshimura, T. et al. Appl Microbiol Biotechnol (2006) 73: 95. doi:10.1007/s00253-006-0437-z


We found a bacterium, Pandoraea sp. 12B-2, of which whole cells catalyzed not only the decarboxylation of 2,6-dihydroxybenzoate but also the regioselective carboxylation of 1,3-dihydroxybenzene to 2,6-dihydroxybenzoate. The whole cells of Pandoraea sp. 12B-2 also catalyzed the regioselective carboxylation of phenol and 1,2-dihydroxybenzene to 4-hydroxybenzoate and 2,3-dihydroxybenzoate, respectively. The molar conversion ratio of the carboxylation reaction depended on the concentration of KHCO3 in the reaction mixture. Only 5 or 48 % of 1,3-dihydroxybenzene added was converted into 2,6-dihydroxybenzoate in the presence of 0.1 M or 3 M KHCO3, respectively. The addition of acetone to the reaction mixture increased the initial rate of the carboxylation reaction, but the final molar conversion yield reached almost the same value. When the efficient production of 2,6-dihydroxybenzoate was optimized using the whole cells of Pandoraea sp. 12B-2, the productivity of 2,6-dihydroxybenzoate topped out at 1.43 M, which was the highest value so far reported. No formation of any other products was observed after the carboxylation reaction.

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© Springer-Verlag 2006