1H, 13C, 15N resonance assignment of the enzyme KdgF from Bacteroides eggerthii
| Autor: | Agnes Beenfeldt Petersen, Idd Andrea Christensen, Mette E. Rønne, Emil G. P. Stender, David Teze, Birte Svensson, Finn Lillelund Aachmann |
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| Jazyk: | angličtina |
| Rok vydání: | 2022 |
| Předmět: | |
| Zdroj: | Petersen, A B, Christensen, I A, Rønne, M E, Stender, E G P, Teze, D, Svensson, B & Aachmann, F L 2022, ' 1 H, 13 C, 15 N resonance assignment of the enzyme KdgF from Bacteroides eggerthii ', Biomolecular N M R Assignments, vol. 16, pp. 343-347 . https://doi.org/10.1007/s12104-022-10102-6 |
| Popis: | 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 1H, 13C, and 15N NMR chemical shift assignment for BeKdgF is reported. |
| Databáze: | OpenAIRE |
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