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Exploring the mechanism of tryptophan 2,3-dioxygenase

The haem proteins TDO (tryptophan 2,3-dioxygenase) and IDO (indoleamine 2,3-dioxygenase) are specific and powerful oxidation catalysts that insert one molecule of dioxygen into L-tryptophan in the first and rate-limiting step in the kynurenine pathway. Recent crystallographic and biochemical analyse...

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Detalles Bibliográficos
Autores principales: Thackray, Sarah J., Mowat, Christopher G., Chapman, Stephen K.
Formato: Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2652831/
https://www.ncbi.nlm.nih.gov/pubmed/19021508
http://dx.doi.org/10.1042/BST0361120
Descripción
Sumario:The haem proteins TDO (tryptophan 2,3-dioxygenase) and IDO (indoleamine 2,3-dioxygenase) are specific and powerful oxidation catalysts that insert one molecule of dioxygen into L-tryptophan in the first and rate-limiting step in the kynurenine pathway. Recent crystallographic and biochemical analyses of TDO and IDO have greatly aided our understanding of the mechanisms employed by these enzymes in the binding and activation of dioxygen and tryptophan. In the present paper, we briefly discuss the function, structure and possible catalytic mechanism of these enzymes.