Biochemical characteristics and inhibitor selectivity of mouse indoleamine 2,3-dioxygenase-2

@article{Austin2010BiochemicalCA,
  title={Biochemical characteristics and inhibitor selectivity of mouse indoleamine 2,3-dioxygenase-2},
  author={Christopher Jonathan Daraius Austin and Boniface Mwongela Mailu and Ghassan J. Maghzal and Angeles Sanchez-Perez and Stefan Rahlfs and Kathleen Zocher and Hajime Julie Yuasa and Jonathan W. Arthur and Katja Becker and Roland Stocker and Nicholas Henry Hunt and Helen J. Ball},
  journal={Amino Acids},
  year={2010},
  volume={39},
  pages={565-578}
}
The first step in the kynurenine pathway of tryptophan catabolism is the cleavage of the 2,3-double bond of the indole ring of tryptophan. In mammals, this reaction is performed independently by indoleamine 2,3-dioxygenase-1 (IDO1), tryptophan 2,3-dioxygenase (TDO) and the recently discovered indoleamine 2,3-dioxygenase-2 (IDO2). Here we describe characteristics of a purified recombinant mouse IDO2 enzyme, including its pH stability, thermal stability and structural features. An improved assay… CONTINUE READING
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