Functional and structural relationship of various extradiol aromatic ring-cleavage dioxygenases of Pseudomonas origin.
The extradiol ring-cleavage dioxygenases derived from seven different Pseudomonas strains were expressed in Escherichia coli and the substrate specificities were investigated for a variety of catecholic compounds. The substrate range of four 2,3-dihydroxybiphenyl dioxygenases from biphenyl-utilizing bacteria, 3-methylcatechol dioxygenase from toluene utilizing Pseudomonas putida F1, 1,2-dihydroxynaphthalene dioxygenase from a NAH7 plasmid, and catechol 2,3-dioxygenase from a TOL plasmid pWW0 were compared. Among the dioxygenases, that from Pseudomonas pseudoalcaligenes KF707 showed a very narrow substrate range. Contrary to this, the dioxygenase from pWW0 showed a relaxed substrate range. The seven extradiol dioxygenases from the various Pseudomonas strains are highly diversified in terms of substrate specificity.
Hirose
J
J
Department of Agricultural Chemistry, Kyushu University, Fukuoka, Japan.
Kimura
N
N
Suyama
A
A
Kobayashi
A
A
Hayashida
S
S
Furukawa
K
K
D001673:Biodegradation, Environmental; D002396:Catechols / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D010105:Oxygenases / Q000235:genetics / Q000378:metabolism*; D011549:Pseudomonas / Q000201:enzymology* / Q000235:genetics; D011994:Recombinant Proteins / Q000378:metabolism; D013045:Species Specificity; D013379:Substrate Specificity
D002396:Catechols; D011994:Recombinant Proteins; D010105:Oxygenases