Purification and characterization of 2,6-dihydroxybenzoate decarboxylase reversibly catalyzing nonoxidative decarboxylation |
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Authors: | Toyokazu?Yoshida Yutaka?Hayakawa Tsuyoshi?Matsui Email author" target="_blank">Toru?NagasawaEmail author |
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Institution: | (1) Department of Biomolecular Science, Gifu University, Yanagido 1-1, Gifu, 501-1193, Japan |
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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%. |
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Keywords: | 2 6-Dihydroxybenzoate decarboxylase 2 6-Dihydroxybenzoate Decarboxylation Carboxylation Agrobacterium tumefaciens IAM12048 |
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