ArticleBiochemistry2010
Spectroscopic studies of ligand and substrate binding to human indoleamine 2,3-dioxygenase.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 40 citations in OpenAlex.
- GAPDH heme delivery to Indoleamine 2,3-dioxygenase 1 involves their complex formation and complementary charge pairing at the protein-protein interface.The Journal of biological chemistry · 2025Article
- Heme-based dioxygenases: Structure, function and dynamics.Journal of inorganic biochemistry · 2024Review
- Indoleamine 2,3-dioxygenase 1 (IDO1): an up-to-date overview of an eclectic immunoregulatory enzyme.The FEBS journal · 2022Review
- One Key and Multiple Locks: Substrate Binding in Structures of Tryptophan Dioxygenases and Hydroxylases.ChemMedChem · 2021Review
- Conformational Plasticity in Human Heme-Based Dioxygenases.Journal of the American Chemical Society · 2021Article
- Kinetic and Spectroscopic Characterization of the Catalytic Ternary Complex of Tryptophan 2,3-Dioxygenase.Biochemistry · 2020Article
- Inhibition Mechanisms of Human Indoleamine 2,3 Dioxygenase 1.Journal of the American Chemical Society · 2018Article
- Structural insights into substrate and inhibitor binding sites in human indoleamine 2,3-dioxygenase 1.Nature communications · 2017Article
- Different Mechanisms of Catalytic Complex Formation in Two L-Tryptophan Processing Dioxygenases.Frontiers in molecular biosciences · 2017Review
- Structural Study of a Flexible Active Site Loop in Human Indoleamine 2,3-Dioxygenase and Its Functional Implications.Biochemistry · 2016Article
- Catalytic activity of human indoleamine 2,3-dioxygenase (hIDO1) at low oxygen.Archives of biochemistry and biophysics · 2015Article
- The mechanism of substrate inhibition in human indoleamine 2,3-dioxygenase.Journal of the American Chemical Society · 2012Article
- NADH oxidase activity of indoleamine 2,3-dioxygenase.The Journal of biological chemistry · 2011Article
- Ferryl derivatives of human indoleamine 2,3-dioxygenase.The Journal of biological chemistry · 2011Article
- Ligand migration in human indoleamine-2,3 dioxygenase.IUBMB life · 2011Article
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
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 in nonhepatic tissues. Steady-state kinetic data showed that hIDO exhibits substrate inhibition behavior, implying the existence of a second substrate binding site in the enzyme, although so far there is no direct evidence supporting it. The kinetic data also revealed that the K(m) of l-Trp (15 microM) is approximately 27-fold lower than the K(d) of l-Trp (0.4 mM) for the ligand-free ferrous enzyme, suggesting that O(2) binding proceeds l-Trp binding during the catalytic cycle. With cyanide as a structural probe, we have investigated the thermodynamic and kinetic parameters associated with ligand and substrate binding to hIDO. Equilibrium titration studies show that the cyanide adduct is capable of binding two l-Trp molecules, with K(d) values of 18 microM and 26 mM. The data offer the first direct evidence of the second substrate binding site in hIDO. Kinetic studies demonstrate that prebinding of l-Trp to the enzyme retards cyanide binding by approximately 13-fold, while prebinding of cyanide to the enzyme facilitates l-Trp binding by approximately 22-fold. The data support the view that during the active turnover of the enzyme it is kinetically more favored to bind O(2) prior to l-Trp.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.