Catalytic properties of the 3-chlorocatechol-oxidizing 2, 3-dihydroxybiphenyl 1,2-dioxygenase from Sphingomonas sp. strain BN6.

@article{Riegert1999CatalyticPO,
  title={Catalytic properties of the 3-chlorocatechol-oxidizing 2, 3-dihydroxybiphenyl 1,2-dioxygenase from Sphingomonas sp. strain BN6.},
  author={Ulrich Riegert and Gesche S Heiss and Andrea Elisabeth Kuhm and Claudia M{\"u}ller and Matthias Contzen and Hans Joachim Knackmuss and Andreas Stolz},
  journal={Journal of bacteriology},
  year={1999},
  volume={181 16},
  pages={4812-7}
}
The 2,3-dihydroxybiphenyl dioxygenase from Sphingomonas sp. strain BN6 (BphC1-BN6) differs from most other extradiol dioxygenases by its ability to oxidize 3-chlorocatechol to 3-chloro-2-hydroxymuconic semialdehyde by a distal cleavage mechanism. The turnover of different substrates and the effects of various inhibitors on BphC1-BN6 were compared with those of another 2,3-dihydroxybiphenyl dioxygenase from the same strain (BphC2-BN6) as well as with those of the archetypical catechol 2,3… CONTINUE READING

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