Purification and crystallization of 2,3-dihydroxybiphenyl 1,2-dioxygenase.

@article{Eltis1993PurificationAC,
  title={Purification and crystallization of 2,3-dihydroxybiphenyl 1,2-dioxygenase.},
  author={Lindsay D Eltis and Birgit Hofmann and Hans J{\"u}rgen Hecht and Heinrich Luensdorf and Kenneth N. Timmis},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 4},
  pages={2727-32}
}
2,3-Dihydroxybiphenyl 1,2-dioxygenase, an enzyme of the biphenyl biodegradation pathway that cleaves the first of the aromatic rings, was purified to apparent homogeneity from Pseudomonas sp. strain LB400 that had been engineered to hyperexpress the bphC gene. The enzyme had a subunit molecular mass of 33.2 kDa as determined by SDS-polyacrylamide electrophoresis. Kinetic studies indicate a KM of 7 +/- 1 microM for 2,3-dihydroxybiphenyl. The enzyme is strongly inhibited by substrate (Kss = 300… CONTINUE READING
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