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  • Title: Functional and structural relationship of various extradiol aromatic ring-cleavage dioxygenases of Pseudomonas origin.
    Author: Hirose J, Kimura N, Suyama A, Kobayashi A, Hayashida S, Furukawa K.
    Journal: FEMS Microbiol Lett; 1994 May 15; 118(3):273-7. PubMed ID: 8020752.
    Abstract:
    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.
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