Binding of L-kynurenine to X. campestris tryptophan 2,3-dioxygenase

Jaswir Basran, Elizabeth S. Booth, Laura P. Campbell, Sarah J. Thackray, Mehul H. Jesani, Jonathan Clayden, Peter C.E. Moody, Christopher G. Mowat, Hanna Kwon*, Emma L. Raven

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

The kynurenine pathway is the major route of tryptophan metabolism. The first step of this pathway is catalysed by one of two heme-dependent dioxygenase enzymes – tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) – leading initially to the formation of N-formylkynurenine (NFK). In this paper, we present a crystal structure of a bacterial TDO from X. campestris in complex with L-kynurenine, the hydrolysed product of NFK. L-kynurenine is bound at the active site in a similar location to the substrate (L-Trp). Hydrogen bonding interactions with Arg117 and the heme 7-propionate anchor the L-kynurenine molecule into the pocket. A mechanism for the hydrolysis of NFK in the active site is presented.

Original languageEnglish
Article number111604
JournalJournal of Inorganic Biochemistry
Early online date16 Sept 2021
Publication statusE-pub ahead of print - 16 Sept 2021

Keywords / Materials (for Non-textual outputs)

  • Heme
  • Kynurenine
  • Tryptophan 2,3-dioxygenase


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