Ligand migration in human indoleamine-2,3 dioxygenase

Karin Nienhaus, Elena Nickel, Changyuan Lu, Syun Ru Yeh, G. Ulrich Nienhaus

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

Human indoleamine 2,3-dioxygenase (hIDO), a monomeric heme enzyme, catalyzes the oxidative degradation of L-tryptophan (L-Trp) and other indoleamine derivatives. Its activity follows typical Michaelis-Menten behavior only for L-Trp concentrations up to 50 μM; a further increase in the concentration of L-Trp causes a decrease in the activity. This substrate inhibition of hIDO is a result of the binding of a second L-Trp molecule in an inhibitory substrate binding site of the enzyme. The molecular details of the reaction and the inhibition are not yet known. In the following, we summarize the present knowledge about this heme enzyme.

Original languageEnglish (US)
Pages (from-to)153-159
Number of pages7
JournalIUBMB Life
Volume63
Issue number3
DOIs
Publication statusPublished - Mar 1 2011

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Keywords

  • FTIR spectroscopy
  • enzyme mechanisms
  • hemeproteins
  • substrate
  • temperature derivative spectroscopy

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics
  • Clinical Biochemistry
  • Cell Biology

Cite this

Nienhaus, K., Nickel, E., Lu, C., Yeh, S. R., & Nienhaus, G. U. (2011). Ligand migration in human indoleamine-2,3 dioxygenase. IUBMB Life, 63(3), 153-159. https://doi.org/10.1002/iub.431