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

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 kineti...

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Auteurs principaux:	Riin Kont, Bastien Bissaro, Vincent G. H. Eijsink, Priit Väljamäe
Format:	article
Langue:	EN
Publié:	Nature Portfolio 2020
Sujets:	Science Q
Accès en ligne:	https://doaj.org/article/cbf3e4be03f74a7aa31fe2d718e0ee9c
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spelling	oai:doaj.org-article:cbf3e4be03f74a7aa31fe2d718e0ee9c2021-12-02T17:32:27ZKinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)10.1038/s41467-020-19561-82041-1723https://doaj.org/article/cbf3e4be03f74a7aa31fe2d718e0ee9c2020-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19561-8https://doaj.org/toc/2041-1723Lytic 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.Riin KontBastien BissaroVincent G. H. EijsinkPriit VäljamäeNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Riin Kont Bastien Bissaro Vincent G. H. Eijsink Priit Väljamäe Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)
description	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.
format	article
author	Riin Kont Bastien Bissaro Vincent G. H. Eijsink Priit Väljamäe
author_facet	Riin Kont Bastien Bissaro Vincent G. H. Eijsink Priit Väljamäe
author_sort	Riin Kont
title	Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)
title_short	Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)
title_full	Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)
title_fullStr	Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)
title_full_unstemmed	Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)
title_sort	kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (lpmos)
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/cbf3e4be03f74a7aa31fe2d718e0ee9c
work_keys_str_mv	AT riinkont kineticinsightsintotheperoxygenaseactivityofcelluloseactivelyticpolysaccharidemonooxygenaseslpmos AT bastienbissaro kineticinsightsintotheperoxygenaseactivityofcelluloseactivelyticpolysaccharidemonooxygenaseslpmos AT vincentgheijsink kineticinsightsintotheperoxygenaseactivityofcelluloseactivelyticpolysaccharidemonooxygenaseslpmos AT priitvaljamae kineticinsightsintotheperoxygenaseactivityofcelluloseactivelyticpolysaccharidemonooxygenaseslpmos
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Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)

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