Hirose J, Kimura N, Suyama A, Kobayashi A, Hayashida S, Furukawa K
Department of Agricultural Chemistry, Kyushu University, Fukuoka, Japan.
FEMS Microbiol Lett. 1994 May 15;118(3):273-7. doi: 10.1111/j.1574-6968.1994.tb06840.x.
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.
从七种不同假单胞菌菌株中获得的二醇裂解双加氧酶在大肠杆菌中表达，并研究了其对多种儿茶酚类化合物的底物特异性。比较了来自联苯利用细菌的四种2,3-二羟基联苯双加氧酶、来自利用甲苯的恶臭假单胞菌F1的3-甲基儿茶酚双加氧酶、来自NAH7质粒的1,2-二羟基萘双加氧酶以及来自TOL质粒pWW0的儿茶酚2,3-双加氧酶的底物范围。在这些双加氧酶中，来自假产碱假单胞菌KF707的双加氧酶底物范围非常狭窄。与此相反，来自pWW0的双加氧酶底物范围较宽。来自不同假单胞菌菌株的七种二醇双加氧酶在底物特异性方面高度多样化。
