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Updated: Aug 30, 2025

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale
Published on: April 19, 2021
1H, 13C, 15N resonance assignment of the enzyme KdgF from Bacteroides eggerthii
Agnes Beenfeldt Petersen1,2, Idd Andrea Christensen2, Mette E Rønne3
1Department of Chemistry, DTU Technical University of Denmark, 2800, Kgs. Lyngby, Denmark.
Abstract:
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.

