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Hirose, J. et al.

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.[1]

References

Functional and structural relationship of various extradiol aromatic ring-cleavage dioxygenases of Pseudomonas origin. Hirose, J., Kimura, N., Suyama, A., Kobayashi, A., Hayashida, S., Furukawa, K. FEMS Microbiol. Lett. (1994) [Pubmed]

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