Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Sarah J. Thackray"'
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
Publikováno v:
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
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 in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c9ed062898cb8f82251351b97a81a35
https://pubmed.ncbi.nlm.nih.gov/34571402
https://pubmed.ncbi.nlm.nih.gov/34571402
Autor:
J. L. Ross Anderson, Stephen K Chapman, Sarah J. Thackray, Emma Lloyd Raven, Christopher G. Mowat, Roman Davydov, Nishma Chauhan, Brian M. Hoffman, Nektaria D. Papadopoulou
Publikováno v:
Journal of the American Chemical Society
Davydov, R M, Chauhan, N, Thackray, S J, Anderson, J L R, Papadopoulou, N D, Mowat, C G, Chapman, S K, Raven, E L & Hoffman, B M 2010, ' Probing the Ternary Complexes of Indoleamine and Tryptophan 2,3-Dioxygenases by Cryoreduction EPR and ENDOR Spectroscopy ', Journal of the American Chemical Society, vol. 132, no. 15, pp. 5494-5500 . https://doi.org/10.1021/ja100518z
Davydov, R M, Chauhan, N, Thackray, S J, Anderson, J L R, Papadopoulou, N D, Mowat, C G, Chapman, S K, Raven, E L & Hoffman, B M 2010, ' Probing the Ternary Complexes of Indoleamine and Tryptophan 2,3-Dioxygenases by Cryoreduction EPR and ENDOR Spectroscopy ', Journal of the American Chemical Society, vol. 132, no. 15, pp. 5494-5500 . https://doi.org/10.1021/ja100518z
We have applied cryoreduction/EPR/ENDOR techniques to characterize the active-site structure of the ferrous-oxy complexes of human (hIDO) and Shewanella oneidensis (sIDO) indoleamine 2,3-dioxygenases, Xanthomonas campestris (XcTDO) tryptophan 2,3-dio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff026c5cd570152556a667e68ef38070
http://europepmc.org/articles/PMC2903012
http://europepmc.org/articles/PMC2903012
Publikováno v:
Biochemical Society Transactions
Thackray, S J, Mowat, C G & Chapman, S K 2008, ' Exploring the mechanism of tryptophan 2,3-dioxygenase ', Biochemical Society Transactions, vol. 36, pp. 1120-1123 . https://doi.org/10.1042/BST0361120
Thackray, S J, Mowat, C G & Chapman, S K 2008, ' Exploring the mechanism of tryptophan 2,3-dioxygenase ', Biochemical Society Transactions, vol. 36, pp. 1120-1123 . https://doi.org/10.1042/BST0361120
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 pathwa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65a66e5cdb8d70d41c54ed7977cffc48
http://europepmc.org/articles/PMC2652831
http://europepmc.org/articles/PMC2652831
Autor:
Igor Efimov, Sandeep Handa, Jaswir Basran, Sarah J. Thackray, Emma Lloyd Raven, Christopher G. Mowat
The heme dioxygenase enzymes involved in tryptophan oxidation catalyse the first and rate-limiting step in the kynurenine pathway—the O 2 -dependent oxidation of l-tryptophan to N -formylkynurenine. In the past 10 years, there have been substantial
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1fbfb13c26efb7032ba0fa0105343ccb
https://doi.org/10.1016/b978-0-12-396462-5.00002-7
https://doi.org/10.1016/b978-0-12-396462-5.00002-7
Autor:
Emma Lloyd Raven, Sandeep Handa, Jaswir Basran, Igor Efimov, Christopher G. Mowat, Sarah J. Thackray
Publikováno v:
Efimov, I, Basran, J, Thackray, S, Handa, S, Mowat, C & Raven, E 2011, ' Structure and Reaction Mechanism in the Heme Dioxygenases ', Biochemistry, vol. 50, pp. 2717-2724 . https://doi.org/10.1021/bi101732n
Biochemistry
Biochemistry
As members of the family of heme-dependent enzymes, the heme dioxygenases are differentiated by virtue of their ability to catalyze the oxidation of l-tryptophan to N-formylkynurenine, the first and rate-limiting step in tryptophan catabolism. In the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20ebc73688212f87746c09e27456b7b9
https://www.pure.ed.ac.uk/ws/files/10366327/Structure_and_Reaction_Mechanism_in_the_Heme_Dioxygenases.pdf
https://www.pure.ed.ac.uk/ws/files/10366327/Structure_and_Reaction_Mechanism_in_the_Heme_Dioxygenases.pdf
Autor:
Farhad Forouhar, Christopher G. Mowat, Sarah J. Thackray, Stephen K Chapman, Liang Tong, Chiara Bruckmann
Publikováno v:
Handbook of Metalloproteins
Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are heme-containing enzymes from a small family of homologous enzymes. Despite both catalyzing the dioxygenation of l-tryptophan, the first step in the kynurenine pathway, the seq
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1ebf7bfe7d23ab86589c28020f4d910a
https://doi.org/10.1002/0470028637.met223
https://doi.org/10.1002/0470028637.met223
Autor:
J.L.R. Anderson, Rong Xiao, Sarah J. Thackray, Chiara Bruckmann, Christopher G. Mowat, Stephen K Chapman, Liang Tong, Li Zhao, Farhad Forouhar, L.P. Campbell
Publikováno v:
Biochemistry. 47(40)
Tryptophan 2,3-dioxygenase (TDO) from Xanthomonas campestris is a highly specific heme-containing enzyme from a small family of homologous enzymes, which includes indoleamine 2,3-dioxygenase (IDO). The structure of wild type (WT TDO) in the catalytic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8511e3c269050119cdb82686a37fac98
https://pubmed.ncbi.nlm.nih.gov/18783250
https://pubmed.ncbi.nlm.nih.gov/18783250
Autor:
Farhad Forouhar, A. Hussain, Rong Xiao, Chiara Bruckmann, J. L. Ross Anderson, Sergey M. Vorobiev, Christopher G. Mowat, Stephen K Chapman, Liang Tong, Gaetano T. Montelione, Li Zhao, Li Chung Ma, Jayaraman Seetharaman, Todd Tucker, Thomas Acton, Mariam Abashidze, Sarah J. Thackray
Publikováno v:
Forouhar, F, Anderson, J L R, Mowat, C, Vorobiev, S, Hussain, A, Abashidze, M, Bruckmann, C, Thackray, S, Seetharaman, J, Tucker, T, Xiao, R, Ma, L, Zhao, L, Acton, T, Montelione, G, Chapman, S & Tong, L 2007, ' Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase ', Proceedings of the National Academy of Sciences, vol. 104, no. 2, pp. 473-478 . https://doi.org/10.1073/pnas.0610007104
Tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) constitute an important, yet relatively poorly understood, family of heme-containing enzymes. Here, we report extensive structural and biochemical studies of the Xanthomonas campe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4da68a6758276796ae8ff3c733bc7ff9
https://hdl.handle.net/20.500.11820/92480326-5567-4646-a1d9-310504e14605
https://hdl.handle.net/20.500.11820/92480326-5567-4646-a1d9-310504e14605
Autor:
Nishma Chauhan, Michael R. F. Lee, Igor Efimov, Emma Lloyd Raven, Jaswir Basran, Sara A. Rafice, Stephen K Chapman, Graham Eaton, Paul R. Jenkins, Sarah J. Thackray, Christopher G. Mowat
Publikováno v:
Journal of the American Chemical Society. 131:4186-4187
Indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) are heme enzymes that catalyze the O(2)-dependent oxidation of L-tryptophan to N-formyl-kynurenine. Previous proposals for the mechanism of this reaction have suggested that depro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c504a81f555a2e3fde8e0f9623dc4437
https://doi.org/10.1021/ja808326g
https://doi.org/10.1021/ja808326g