title: Ligand migration in human indoleamine-2,3 dioxygenase.
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.
authors: Karlsruhe Institute of Technology (KIT), Institute of Applied Physics and Center for Functional Nanostructures, Karlsruhe, Germany. Karin.nienhaus@kit.edu
authors: Karin
authors: K
authors: Nienhaus
authors: Elena
authors: E
authors: Nickel
authors: Changyuan
authors: C
authors: Lu
authors: Syun-Ru
authors: SR
authors: Yeh
authors: G Ulrich
authors: GU
authors: Nienhaus
mesh_terms: D055162:Biocatalysis; D006801:Humans; D050503:Indoleamine-Pyrrole 2,3,-Dioxygenase / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D008024:Ligands; D008958:Models, Molecular; D013379:Substrate Specificity
chemical_list: D050503:Indoleamine-Pyrrole 2,3,-Dioxygenase; D008024:Ligands