Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)

Riin Kont; Bastien Bissaro; Vincent G. H. Eijsink; Priit Väljamäe

doi:10.1038/s41467-020-19561-8

Nature Communications (Nov 2020)

Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)

Riin Kont,
Bastien Bissaro,
Vincent G. H. Eijsink,
Priit Väljamäe

Affiliations

Riin Kont: Institute of Molecular and Cell Biology, University of Tartu
Bastien Bissaro: Faculty of Chemistry, Biotechnology and Food Science, NMBU—Norwegian University of Life Sciences
Vincent G. H. Eijsink: Faculty of Chemistry, Biotechnology and Food Science, NMBU—Norwegian University of Life Sciences
Priit Väljamäe: Institute of Molecular and Cell Biology, University of Tartu

DOI: https://doi.org/10.1038/s41467-020-19561-8
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 10

Abstract

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Lytic polysaccharide monooxygenases (LPMOs) catalyze the hydroxylation of glycosidic bonds in polysaccharides, but the catalytic properties of these monocopper enzymes remain poorly characterized. Here authors employ competition between reference enzymes and LPMOs for the H2O2 co-substrate to kinetically characterize LPMO-catalyzed cellulose oxidation.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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