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- Title
Purification and characterization of 2,6-dihydroxybenzoate decarboxylase reversibly catalyzing nonoxidative decarboxylation.
- Authors
Yoshida, Toyokazu; Hayakawa, Yutaka; Matsui, Tsuyoshi; Nagasawa, Toru
- 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%.
- Subjects
AGROBACTERIUM tumefaciens; DECARBOXYLATION; OXIDATION; ENZYMES; AGROBACTERIUM; ELIMINATION reactions
- Publication
Archives of Microbiology, 2004, Vol 181, Issue 6, p391
- ISSN
0302-8933
- Publication type
Article
- DOI
10.1007/s00203-004-0668-2