Purification and characterization of 2,6-dihydroxybenzoate decarboxylase reversibly catalyzing nonoxidative decarboxylation.
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 KHCO(3), the enzyme also catalyzed the regioselective carboxylation of 1,3-dihydroxybenzene into 2,6-dihydroxybenzoate at a molar conversion ratio of 30%.
Yoshida
Toyokazu
T
Department of Biomolecular Science, Gifu University, Yanagido 1-1, 501-1193, Gifu, Japan.
Hayakawa
Yutaka
Y
Matsui
Tsuyoshi
T
Nagasawa
Toru
T
D016960:Agrobacterium tumefaciens / Q000201:enzymology*; D001639:Bicarbonates / Q000378:metabolism; D002262:Carboxy-Lyases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D003067:Coenzymes; D003653:Decarboxylation; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D062385:Hydroxybenzoates / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D017680:Potassium Compounds / Q000378:metabolism; D021122:Protein Subunits / Q000737:chemistry; D012118:Resorcinols / Q000378:metabolism; D013237:Stereoisomerism; D013379:Substrate Specificity
D001639:Bicarbonates; D003067:Coenzymes; D062385:Hydroxybenzoates; D017680:Potassium Compounds; D021122:Protein Subunits; D012118:Resorcinols; C009135:2,3-dihydroxybenzoic acid; C488807:2,6-dihydroxybenzoate decarboxylase; D002262:Carboxy-Lyases; C026329:potassium bicarbonate; C412605:gamma-resorcylic acid