Cargando…
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...
Autores principales: | , , |
---|---|
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 |
_version_ | 1782165255293501440 |
---|---|
author | Thackray, Sarah J. Mowat, Christopher G. Chapman, Stephen K. |
author_facet | Thackray, Sarah J. Mowat, Christopher G. Chapman, Stephen K. |
author_sort | Thackray, Sarah J. |
collection | PubMed |
description | 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. |
format | Text |
id | pubmed-2652831 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-26528312009-03-09 Exploring the mechanism of tryptophan 2,3-dioxygenase Thackray, Sarah J. Mowat, Christopher G. Chapman, Stephen K. Biochem Soc Trans Biochemical Society Focused Meetings 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. Portland Press Ltd. 2008-11-19 2008-12-01 /pmc/articles/PMC2652831/ /pubmed/19021508 http://dx.doi.org/10.1042/BST0361120 Text en © 2008 The Author(s) The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Non-Commercial Licence (http://creativecommons.org/licenses/by-nc/2.5/) which permits unrestricted non-commercial use, distribution and reproduction in any medium, provided the original work is properly cited. http://creativecommons.org/licenses/by-nc/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Biochemical Society Focused Meetings Thackray, Sarah J. Mowat, Christopher G. Chapman, Stephen K. Exploring the mechanism of tryptophan 2,3-dioxygenase |
title | Exploring the mechanism of tryptophan 2,3-dioxygenase |
title_full | Exploring the mechanism of tryptophan 2,3-dioxygenase |
title_fullStr | Exploring the mechanism of tryptophan 2,3-dioxygenase |
title_full_unstemmed | Exploring the mechanism of tryptophan 2,3-dioxygenase |
title_short | Exploring the mechanism of tryptophan 2,3-dioxygenase |
title_sort | exploring the mechanism of tryptophan 2,3-dioxygenase |
topic | Biochemical Society Focused Meetings |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2652831/ https://www.ncbi.nlm.nih.gov/pubmed/19021508 http://dx.doi.org/10.1042/BST0361120 |
work_keys_str_mv | AT thackraysarahj exploringthemechanismoftryptophan23dioxygenase AT mowatchristopherg exploringthemechanismoftryptophan23dioxygenase AT chapmanstephenk exploringthemechanismoftryptophan23dioxygenase |