Mouse and human indoleamine 2,3-dioxygenase display some distinct biochemical and structural properties

@article{Austin2008MouseAH,
  title={Mouse and human indoleamine 2,3-dioxygenase display some distinct biochemical and structural properties},
  author={Christopher Jonathan Daraius Austin and Florian Astelbauer and Priambudi Kosim-Satyaputra and Helen J. Ball and Robert D. Willows and Joanne F Jamie and Nicholas Henry Hunt},
  journal={Amino Acids},
  year={2008},
  volume={36},
  pages={99-106}
}
The hemoprotein indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting enzyme in the most significant pathway for mammalian tryptophan metabolism. It has received considerable attention in recent years, particularly due to its dual role in immunity and the pathogenesis of many diseases. Reported here are differences and similarities between biochemical behaviour and structural features of recombinant human IDO and recombinant mouse IDO. Significant differences were observed in the… CONTINUE READING

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