Characterization of catechol 2,3-dioxygenases.
Three catechol 2,3-dioxygenases for biphenyl, naphthalene/salicylate, and toluene/xylene oxidation were cloned from Achromobacter xylosoxidans KF701, Pseudomonas putida (NAH7), and Pseudomonas sp. (pWWO). The cloned catechol 2,3-dioxygenases were identified by enzymatic activity assay in addition to yellow bands on polyacrylamide gel after electrophoresis and activity staining. All of the cloned catechol 2,3-dioxygenases exhibited their highest activities on catechol as a substrate compared with catechol derivatives including 4-chlorocatechol, 3-methylcatechol, and 4-methylcatechol. The cloned catechol 2,3-dioxygenases are not fused proteins but were significantly different from one another in their electrophoretic mobilities on nondenaturing 7.5%-polyacrylamide gel.
Kim
Y
Y
Department of Biochemistry, College of Pharmacy, Chungbuk National University, Cheongju, Korea.
Choi
B
B
Lee
J
J
Chang
H
H
Min
K R
KR
D000421:Alcaligenes / Q000235:genetics*; D050557:Catechol 2,3-Dioxygenase; D003001:Cloning, Molecular; D049308:Dioxygenases; D010105:Oxygenases / Q000737:chemistry / Q000235:genetics*; D011549:Pseudomonas / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D015183:Restriction Mapping
D011994:Recombinant Proteins; D010105:Oxygenases; D049308:Dioxygenases; D050557:Catechol 2,3-Dioxygenase