Binding of l-kynurenine to X. campestris tryptophan 2,3-dioxygenase
| Autor: | Mehul H. Jesani, Jonathan Clayden, Laura P. Campbell, Sarah J. Thackray, Jaswir Basran, Peter C. E. Moody, Emma Lloyd Raven, Elizabeth S. Booth, Christopher G. Mowat, Hanna Kwon |
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| Rok vydání: | 2021 |
| Předmět: |
Kynurenine pathway
Stereochemistry Iron Heme Xanthomonas campestris Biochemistry Inorganic Chemistry Tryptophan 2 3-dioxygenase chemistry.chemical_compound Dioxygenase Kynurenine chemistry.chemical_classification biology Tryptophan Active site Substrate (chemistry) Hydrogen Bonding Stereoisomerism Tryptophan Oxygenase Enzyme chemistry biology.protein Oxidation-Reduction Protein Binding |
| Zdroj: | Basran, J, Booth, E S, Campbell, L P, Thackray, S J, Jesani, M H, Clayden, J, Moody, P C E, Mowat, C G, Kwon, H & Raven, E L 2021, ' Binding of L-kynurenine to X. campestris tryptophan 2,3-dioxygenase ', Journal of Inorganic Biochemistry, vol. 225, 111604 . https://doi.org/10.1016/j.jinorgbio.2021.111604 |
| ISSN: | 1873-3344 |
| DOI: | 10.1016/j.jinorgbio.2021.111604 |
| Popis: | The kynurenine pathway is the major route of tryptophan metabolism. The first step of this pathway is catalysed by one of two heme-dependent dioxygenase enzymes – tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) – leading initially to the formation of N-formylkynurenine (NFK). In this paper, we present a crystal structure of a bacterial TDO from X. campestris in complex with L-kynurenine, the hydrolysed product of NFK. L-kynurenine is bound at the active site in a similar location to the substrate (L-Trp). Hydrogen bonding interactions with Arg117 and the heme 7-propionate anchor the L-kynurenine molecule into the pocket. A mechanism for the hydrolysis of NFK in the active site is presented. |
| Databáze: | OpenAIRE |
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