Characterization and evolution of anthranilate 1,2-dioxygenase from Acinetobacter sp. strain ADP1.

@article{Eby2001CharacterizationAE,
  title={Characterization and evolution of anthranilate 1,2-dioxygenase from Acinetobacter sp. strain ADP1.},
  author={D Matthew Eby and Zanna M Beharry and Eric D. Coulter and Donald M Kurtz and Ellen L Neidle},
  journal={Journal of bacteriology},
  year={2001},
  volume={183 1},
  pages={109-18}
}
The two-component anthranilate 1,2-dioxygenase of the bacterium Acinetobacter sp. strain ADP1 was expressed in Escherichia coli and purified to homogeneity. This enzyme converts anthranilate (2-aminobenzoate) to catechol with insertion of both atoms of O(2) and consumption of one NADH. The terminal oxygenase component formed an alpha(3)beta(3) hexamer of 54- and 19-kDa subunits. Biochemical analyses demonstrated one Rieske-type [2Fe-2S] center and one mononuclear nonheme iron center in each… CONTINUE READING

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