Abstract
The lytic polysaccharide monooxygenase JdLPMO10A is the N-terminal domain of the multimodular protein Jd1381. The isolated JdLPMO10A domain is one of the smallest chitin-active lytic polysaccharide monooxygenases known to date with a size of only 15.5 kDa. JdLPMO10A is a copper-dependent oxidative enzyme that depolymerizes chitin by hydroxylating the C1 carbon in the glycosidic bond. JdLPMO10A has been isotopically labeled and recombinantly expressed. Here, we report the 1H, 13C, 15N resonance assignment of JdLPMO10A. Secondary structural elements predicted based on the NMR assignment are in excellent agreement with the crystal structure of JdLPMO10A.
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Acknowledgements
This work was financed by the Novo Nordisk Foundation (grant number NNF18OC0032242), the OXYMOD project, the Norwegian NMR Platform and a FRIPRO project (grants 269408, 226244 and 262853 from the Research Council of Norway, respectively).
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Christensen, I.A., Eijsink, V.G.H., Aachmann, F.L. et al. 1H, 13C, 15N resonance assignment of the apo form of the small, chitin-active lytic polysaccharide monooxygenase JdLPMO10A from Jonesia denitrificans. Biomol NMR Assign 15, 79–84 (2021). https://doi.org/10.1007/s12104-020-09986-z
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DOI: https://doi.org/10.1007/s12104-020-09986-z