Expression of rat liver tryptophan 2,3-dioxygenase in Escherichia coli: structural and functional characterization of the purified enzyme.

@article{Ren1996ExpressionOR,
  title={Expression of rat liver tryptophan 2,3-dioxygenase in Escherichia coli: structural and functional characterization of the purified enzyme.},
  author={Shun-xiang Ren and Hongmei Liu and E Licad and Maria Almira Correia},
  journal={Archives of biochemistry and biophysics},
  year={1996},
  volume={333 1},
  pages={96-102}
}
The hepatic hemoprotein tryptophan 2,3-dioxygenase (TDO) is the key regulatory enzyme that, through irreversible degradation, controls the flux of tryptophan through physiologically relevant pathways. This enzyme is composed of four identical subunits and in its fully assembled tetrameric form requires 2 mol of heme (Fe(+2)-protoporphyrin IX)/mol of protein for functional competence. Using a full-length cDNA for the rat liver TDO subunit (pUC119/TDO) as the template, TDO cDNA was amplified by… CONTINUE READING

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