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(1)H, (15)N, (13)C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol

Catechol O-methyltransferase (COMT) is an enzyme that plays a major role in catechol neurotransmitter deactivation. Inhibition of COMT can increase neurotransmitter levels, which provides a means of treatment for Parkinson’s disease, schizophrenia and depression. COMT exists as two isozymes: a solub...

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Autores principales: Czarnota, Sylwia, Baxter, Nicola J., Cliff, Matthew J., Waltho, Jonathan P., Scrutton, Nigel S., Hay, Sam
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5343089/
https://www.ncbi.nlm.nih.gov/pubmed/27981425
http://dx.doi.org/10.1007/s12104-016-9720-9
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author Czarnota, Sylwia
Baxter, Nicola J.
Cliff, Matthew J.
Waltho, Jonathan P.
Scrutton, Nigel S.
Hay, Sam
author_facet Czarnota, Sylwia
Baxter, Nicola J.
Cliff, Matthew J.
Waltho, Jonathan P.
Scrutton, Nigel S.
Hay, Sam
author_sort Czarnota, Sylwia
collection PubMed
description Catechol O-methyltransferase (COMT) is an enzyme that plays a major role in catechol neurotransmitter deactivation. Inhibition of COMT can increase neurotransmitter levels, which provides a means of treatment for Parkinson’s disease, schizophrenia and depression. COMT exists as two isozymes: a soluble cytoplasmic form (S-COMT), expressed in the liver and kidneys and a membrane-bound form (MB-COMT), found mostly in the brain. Here we report the backbone (1)H, (15)N and (13)C chemical shift assignments of S-COMT in complex with S-adenosyl-l-methionine, 3,5-dinitrocatechol and Mg(2+). Assignments were obtained by heteronuclear multidimensional NMR spectroscopy. In total, 97 % of all backbone resonances were assigned in the complex, with 205 out of a possible 215 residues assigned in the (1)H-(15)N TROSY spectrum. Prediction of solution secondary structure from a chemical shift analysis using the TALOS+ webserver is in good agreement with published X-ray crystal structures.
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spelling pubmed-53430892017-03-21 (1)H, (15)N, (13)C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol Czarnota, Sylwia Baxter, Nicola J. Cliff, Matthew J. Waltho, Jonathan P. Scrutton, Nigel S. Hay, Sam Biomol NMR Assign Article Catechol O-methyltransferase (COMT) is an enzyme that plays a major role in catechol neurotransmitter deactivation. Inhibition of COMT can increase neurotransmitter levels, which provides a means of treatment for Parkinson’s disease, schizophrenia and depression. COMT exists as two isozymes: a soluble cytoplasmic form (S-COMT), expressed in the liver and kidneys and a membrane-bound form (MB-COMT), found mostly in the brain. Here we report the backbone (1)H, (15)N and (13)C chemical shift assignments of S-COMT in complex with S-adenosyl-l-methionine, 3,5-dinitrocatechol and Mg(2+). Assignments were obtained by heteronuclear multidimensional NMR spectroscopy. In total, 97 % of all backbone resonances were assigned in the complex, with 205 out of a possible 215 residues assigned in the (1)H-(15)N TROSY spectrum. Prediction of solution secondary structure from a chemical shift analysis using the TALOS+ webserver is in good agreement with published X-ray crystal structures. Springer Netherlands 2016-12-15 2017 /pmc/articles/PMC5343089/ /pubmed/27981425 http://dx.doi.org/10.1007/s12104-016-9720-9 Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Article
Czarnota, Sylwia
Baxter, Nicola J.
Cliff, Matthew J.
Waltho, Jonathan P.
Scrutton, Nigel S.
Hay, Sam
(1)H, (15)N, (13)C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol
title (1)H, (15)N, (13)C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol
title_full (1)H, (15)N, (13)C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol
title_fullStr (1)H, (15)N, (13)C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol
title_full_unstemmed (1)H, (15)N, (13)C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol
title_short (1)H, (15)N, (13)C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol
title_sort (1)h, (15)n, (13)c backbone resonance assignments of human soluble catechol o-methyltransferase in complex with s-adenosyl-l-methionine and 3,5-dinitrocatechol
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5343089/
https://www.ncbi.nlm.nih.gov/pubmed/27981425
http://dx.doi.org/10.1007/s12104-016-9720-9
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