Archives of Microbiology

, Volume 181, Issue 6, pp 391–397

Purification and characterization of 2,6-dihydroxybenzoate decarboxylase reversibly catalyzing nonoxidative decarboxylation

  • Toyokazu Yoshida
  • Yutaka Hayakawa
  • Tsuyoshi Matsui
  • Toru Nagasawa
Original Paper

DOI: 10.1007/s00203-004-0668-2

Cite this article as:
Yoshida, T., Hayakawa, Y., Matsui, T. et al. Arch Microbiol (2004) 181: 391. doi:10.1007/s00203-004-0668-2

Abstract

A nonoxidative decarboxylase, 2,6-dihydroxybenzoate decarboxylase, was found in Agrobacterium tumefaciens IAM12048. The enzyme activity was induced specifically by 2,6-dihydroxybenzoate. The purified enzyme was a homotetramer of identical 38 kDa subunits. The purified decarboxylase catalyzed the nonoxidative decarboxylation of 2,6-dihydroxybenzoate and 2,3-dihydroxybenzoate without requiring any cofactors. In the presence of KHCO3, the enzyme also catalyzed the regioselective carboxylation of 1,3-dihydroxybenzene into 2,6-dihydroxybenzoate at a molar conversion ratio of 30%.

Keywords

2,6-Dihydroxybenzoate decarboxylase 2,6-Dihydroxybenzoate Decarboxylation Carboxylation Agrobacterium tumefaciens IAM12048 

Copyright information

© Springer-Verlag 2004

Authors and Affiliations

  • Toyokazu Yoshida
    • 1
  • Yutaka Hayakawa
    • 1
  • Tsuyoshi Matsui
    • 1
  • Toru Nagasawa
    • 1
  1. 1.Department of Biomolecular ScienceGifu UniversityGifuJapan

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