Biotechnology Letters

, Volume 32, Issue 5, pp 701–705 | Cite as

Regioselective carboxylation of catechol by 3,4-dihydroxybenzoate decarboxylase of Enterobacter cloacae P

  • Toyokazu Yoshida
  • Yuki Inami
  • Tsuyoshi Matsui
  • Toru Nagasawa
Original Research Paper

Abstract

3,4-Dihydroxybenzoate decarboxylase in Enterobacter cloacae P241 was induced by adding 3,4-dihydroxybenzoic acid, 3-hydroxybenzoic acid, 3,4,5-trihydroxybenzoic acid or 4-acetamidobenzoic acid to the culture medium. After stabilizing the enzyme activity by adding 5 mM dithiothreitol and 20 mM Na2S2O3 to a cell-free extract, catechol at 50 mM was carboxylated in the presence of 3 M KHCO3 to 3,4-dihydroxybenzoic acid with a molar conversion ratio of 28% after 14 h at 30°C.

Keywords

Carboxylation Catechol 3,4-Dihydroxybenzoate decarboxylase Enterobacter cloacae 

References

  1. Gorny N, Schink B (1994) Anaerobic degradation of catechol by Desulfobacterium sp. strain Cat2 proceeds via carboxylation to protocatechuate. Appl Environ Microbiol 60:3396–3400PubMedGoogle Scholar
  2. He Z, Wiegel J (1995) Purification and characterization of an oxygen-sensitive reversible 4-hydroxybenzoate decarboxylase from Clostridium hydroxybenzoicum. Eur J Biochem 229:77–82CrossRefPubMedGoogle Scholar
  3. He Z, Wiegel J (1996) Purification and characterization of an oxygen-sensitive 3,4-dihydroxybenzoate decarboxylase from Clostridium hydroxybenzoicum. J Bacteriol 178:3539–3543PubMedGoogle Scholar
  4. Johnson R, Colwell RR, Sakazaki R, Tamura K (1975) Numerical study of the Enterobacter. Int J Syst Bacteriol 25:12–37CrossRefGoogle Scholar
  5. Matsui T, Yoshida T, Yoshimura T, Nagasawa T (2006a) Regioselective carboxylation of 1,3-dihydroxybenzene by 2,6-dihydroxybenzoate decarboxylase of Pandoraea sp. 12B–2. Appl Microbiol Biotechnol 73:95–102CrossRefPubMedGoogle Scholar
  6. Matsui T, Yoshida T, Hayashi T, Nagasawa T (2006b) Purification, characterization and gene cloning of 4-hydroxybenzoate decarboxylase of Enterobacter cloacae P240. Arch Microbiol 186:21–29CrossRefPubMedGoogle Scholar
  7. Omura H, Wieser M, Nagasawa T (1998) Pyrrole-2-carboxylate decarboxylase from Bacillus megaterium PYR2910, an organic-acid-requiring enzyme. Eur J Biochem 253:480–484CrossRefPubMedGoogle Scholar
  8. Uchida A, Ogawa M, Yoshida T, Nagasawa T (2003) Quinolinate dehydrogenase and 6-hydroxyquinolinate decarboxylase involved in the conversion of quinolinic acid to 6-hydroxynicotinic acid by Alcaligenes sp. UK21. Arch Microbiol 180:81–87CrossRefPubMedGoogle Scholar
  9. Wieser M, Fujii N, Yoshida T, Nagasawa T (1998) Carbon dioxide fixation by reversible pyrrole-2-carboxylate decarboxylase from Bacillus megaterium PYR2910. Eur J Biochem 257:495–499CrossRefPubMedGoogle Scholar
  10. Yoshida T, Fujita K, Nagasawa T (2002) Novel reversible indole-3-carboxylate decarboxylase catalyzing nonoxidative decarboxylation. Biosci Biotechnol Biochem 66:2388–2394CrossRefPubMedGoogle Scholar
  11. Yoshida T, Hayakawa Y, Matsui T, Nagasawa T (2004) Purification and characterization of 2,6-dihydroxybenzoate decarboxylase reversibly catalyzing nonoxidative decarboxylation. Arch Microbiol 181:391–397CrossRefPubMedGoogle Scholar

Copyright information

© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  • Toyokazu Yoshida
    • 1
  • Yuki Inami
    • 1
  • Tsuyoshi Matsui
    • 1
  • Toru Nagasawa
    • 1
  1. 1.Department of Biomolecular ScienceGifu UniversityGifuJapan

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