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Ligand migration in human indoleamine-2,3 dioxygenase

✍ Scribed by Karin Nienhaus; Elena Nickel; Changyuan Lu; Syun-Ru Yeh; G. Ulrich Nienhaus

Publisher
John Wiley and Sons
Year
2011
Tongue
English
Weight
430 KB
Volume
63
Category
Article
ISSN
1521-6543

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✦ Synopsis

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. © 2011 IUBMB IUBMB Life, 63(3): 153–159, 2011

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