Mechanistic basis of substrate-O
EPR
NMR
chitin
copper
lytic polysaccharide monooxygenase
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
11 08 2020
11 08 2020
Historique:
pubmed:
30
7
2020
medline:
21
10
2020
entrez:
30
7
2020
Statut:
ppublish
Résumé
Lytic polysaccharide monooxygenases (LPMOs) have a unique ability to activate molecular oxygen for subsequent oxidative cleavage of glycosidic bonds. To provide insight into the mode of action of these industrially important enzymes, we have performed an integrated NMR/electron paramagnetic resonance (EPR) study into the detailed aspects of an AA10 LPMO-substrate interaction. Using NMR spectroscopy, we have elucidated the solution-phase structure of
Identifiants
pubmed: 32723819
pii: 2004277117
doi: 10.1073/pnas.2004277117
pmc: PMC7431007
doi:
Substances chimiques
Bacterial Proteins
0
Chitin
1398-61-4
Copper
789U1901C5
Mixed Function Oxygenases
EC 1.-
Oxygen
S88TT14065
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
19178-19189Subventions
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/L001926/1
Pays : United Kingdom
Informations de copyright
Copyright © 2020 the Author(s). Published by PNAS.
Déclaration de conflit d'intérêts
The authors declare no competing interest.
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