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1H, 13C, 15N resonance assignment of the apo form of the small, chitin-active lytic polysaccharide monooxygenase JdLPMO10Afrom Jonesia denitrificans

Christensen, Idd Andrea; Eijsink, Vincent; Aachmann, Finn Lillelund; Courtade, Gaston
Peer reviewed, Journal article
Accepted version
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URI
https://hdl.handle.net/11250/2772081
Date
2020
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  • Institutt for bioteknologi og matvitenskap [1690]
  • Publikasjoner fra CRIStin - NTNU [41881]
Original version
10.1007/s12104-020-09986-z
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.
Publisher
Springer
Journal
Biomolecular NMR Assignments

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