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Ligand Migration in Human Indoleamine-2,3 Dioxygenase

Nienhaus, K. 1; Nickel, E. 1; Lu, C.; Yeh, S.-R.; Nienhaus, G. U. ORCID iD icon 1
1 Institut für Angewandte Physik (APH), Karlsruher Institut für Technologie (KIT)

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 mi 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.


Scopus
Zitationen: 8
Web of Science
Zitationen: 8
Zugehörige Institution(en) am KIT Institut für Angewandte Physik (APH)
Publikationstyp Zeitschriftenaufsatz
Publikationsjahr 2011
Sprache Englisch
Identifikator ISSN: 1521-6543
KITopen-ID: 1000027131
Erschienen in IUBMB Life
Verlag John Wiley and Sons
Band 63
Heft 3
Seiten 153 - 159
Nachgewiesen in Scopus
Web of Science
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