(1)H, (13)C, (15)N resonance assignment of the enzyme KdgF from Bacteroides eggerthii

To fully utilize carbohydrates from seaweed biomass, the degradation of the family of polysaccharides known as alginates must be understood. A step in the degradation of alginate is the conversion of 4,5-unsaturated monouronates to 4-deoxy-L-erythro-5-hexoseulose catalysed by the enzyme KdgF. In thi...

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Autores principales: Petersen, Agnes Beenfeldt, Christensen, Idd Andrea, Rønne, Mette E., Stender, Emil G. P., Teze, David, Svensson, Birte, Aachmann, Finn Lillelund
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2022
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9510102/
https://www.ncbi.nlm.nih.gov/pubmed/36042150
http://dx.doi.org/10.1007/s12104-022-10102-6
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author Petersen, Agnes Beenfeldt
Christensen, Idd Andrea
Rønne, Mette E.
Stender, Emil G. P.
Teze, David
Svensson, Birte
Aachmann, Finn Lillelund
author_facet Petersen, Agnes Beenfeldt
Christensen, Idd Andrea
Rønne, Mette E.
Stender, Emil G. P.
Teze, David
Svensson, Birte
Aachmann, Finn Lillelund
author_sort Petersen, Agnes Beenfeldt
collection PubMed
description To fully utilize carbohydrates from seaweed biomass, the degradation of the family of polysaccharides known as alginates must be understood. A step in the degradation of alginate is the conversion of 4,5-unsaturated monouronates to 4-deoxy-L-erythro-5-hexoseulose catalysed by the enzyme KdgF. In this study BeKdgF from Bacteroides eggerthii from the human gut microbiota has been produced isotopically labelled in Escherichia coli. Here the (1)H, (13)C, and (15)N NMR chemical shift assignment for BeKdgF is reported.
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spelling pubmed-95101022022-09-27 (1)H, (13)C, (15)N resonance assignment of the enzyme KdgF from Bacteroides eggerthii Petersen, Agnes Beenfeldt Christensen, Idd Andrea Rønne, Mette E. Stender, Emil G. P. Teze, David Svensson, Birte Aachmann, Finn Lillelund Biomol NMR Assign Article To fully utilize carbohydrates from seaweed biomass, the degradation of the family of polysaccharides known as alginates must be understood. A step in the degradation of alginate is the conversion of 4,5-unsaturated monouronates to 4-deoxy-L-erythro-5-hexoseulose catalysed by the enzyme KdgF. In this study BeKdgF from Bacteroides eggerthii from the human gut microbiota has been produced isotopically labelled in Escherichia coli. Here the (1)H, (13)C, and (15)N NMR chemical shift assignment for BeKdgF is reported. Springer Netherlands 2022-08-30 2022 /pmc/articles/PMC9510102/ /pubmed/36042150 http://dx.doi.org/10.1007/s12104-022-10102-6 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Petersen, Agnes Beenfeldt
Christensen, Idd Andrea
Rønne, Mette E.
Stender, Emil G. P.
Teze, David
Svensson, Birte
Aachmann, Finn Lillelund
(1)H, (13)C, (15)N resonance assignment of the enzyme KdgF from Bacteroides eggerthii
title (1)H, (13)C, (15)N resonance assignment of the enzyme KdgF from Bacteroides eggerthii
title_full (1)H, (13)C, (15)N resonance assignment of the enzyme KdgF from Bacteroides eggerthii
title_fullStr (1)H, (13)C, (15)N resonance assignment of the enzyme KdgF from Bacteroides eggerthii
title_full_unstemmed (1)H, (13)C, (15)N resonance assignment of the enzyme KdgF from Bacteroides eggerthii
title_short (1)H, (13)C, (15)N resonance assignment of the enzyme KdgF from Bacteroides eggerthii
title_sort (1)h, (13)c, (15)n resonance assignment of the enzyme kdgf from bacteroides eggerthii
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9510102/
https://www.ncbi.nlm.nih.gov/pubmed/36042150
http://dx.doi.org/10.1007/s12104-022-10102-6
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