Inhibitory substrate binding site of human indoleamine 2,3-dioxygenase

Changyuan Lu, Yu Lin, Syun Ru Yeh

Research output: Contribution to journalArticlepeer-review

76 Scopus citations


(Graph Presented) Human indoleamine 2,3-dioxygenase (hIDO) is an intracellular heme-containing enzyme, which catalyzes the initial and rate-determining step of L-tryptophan (L-Trp) metabolism via the kynurenine pathway. Due to its immunosuppressive function, hIDO has been recognized as an important drug target for cancer. Here we report evidence supporting the presence of an inhibitory substrate binding site (Si) in hIDO that is capable of binding molecules with a wide variety of structures, including substrates (L-Trp and 1-methyl-L-tryptophan), an effector (3-indole ethanol), and an uncompetitive inhibitor (Mitomycin C). The data offer useful guidelines for future development of more potent hIDO inhibitors; they also call for the re-evaluation of the action mechanism of Mitomycin C (MtoC), a widely used antitumor chemotherapeutic agent.

Original languageEnglish (US)
Pages (from-to)12866-12867
Number of pages2
JournalJournal of the American Chemical Society
Issue number36
StatePublished - Sep 16 2009

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry


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