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On the impact of carbohydrate-binding modules (CBMs) in lytic polysaccharide monooxygenases (LPMOs)

Lytic polysaccharide monooxygenases (LPMOs) have revolutionized our understanding of how enzymes degrade insoluble polysaccharides. Compared with the substantial knowledge developed on the structure and mode of action of the catalytic LPMO domains, the (multi)modularity of LPMOs has received less at...

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Autores principales: Forsberg, Zarah, Courtade, Gaston
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10154629/
https://www.ncbi.nlm.nih.gov/pubmed/36504118
http://dx.doi.org/10.1042/EBC20220162
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author Forsberg, Zarah
Courtade, Gaston
author_facet Forsberg, Zarah
Courtade, Gaston
author_sort Forsberg, Zarah
collection PubMed
description Lytic polysaccharide monooxygenases (LPMOs) have revolutionized our understanding of how enzymes degrade insoluble polysaccharides. Compared with the substantial knowledge developed on the structure and mode of action of the catalytic LPMO domains, the (multi)modularity of LPMOs has received less attention. The presence of other domains, in particular carbohydrate-binding modules (CBMs), tethered to LPMOs has profound implications for the catalytic performance of the full-length enzymes. In the last few years, studies on LPMO modularity have led to advancements in elucidating how CBMs, other domains, and linker regions influence LPMO structure and function. This mini review summarizes recent literature, with particular focus on comparative truncation studies, to provide an overview of the diversity in LPMO modularity and the functional implications of this diversity.
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spelling pubmed-101546292023-05-04 On the impact of carbohydrate-binding modules (CBMs) in lytic polysaccharide monooxygenases (LPMOs) Forsberg, Zarah Courtade, Gaston Essays Biochem Enzymology Lytic polysaccharide monooxygenases (LPMOs) have revolutionized our understanding of how enzymes degrade insoluble polysaccharides. Compared with the substantial knowledge developed on the structure and mode of action of the catalytic LPMO domains, the (multi)modularity of LPMOs has received less attention. The presence of other domains, in particular carbohydrate-binding modules (CBMs), tethered to LPMOs has profound implications for the catalytic performance of the full-length enzymes. In the last few years, studies on LPMO modularity have led to advancements in elucidating how CBMs, other domains, and linker regions influence LPMO structure and function. This mini review summarizes recent literature, with particular focus on comparative truncation studies, to provide an overview of the diversity in LPMO modularity and the functional implications of this diversity. Portland Press Ltd. 2023-04 2023-04-18 /pmc/articles/PMC10154629/ /pubmed/36504118 http://dx.doi.org/10.1042/EBC20220162 Text en © 2023 The Author(s). https://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Enzymology
Forsberg, Zarah
Courtade, Gaston
On the impact of carbohydrate-binding modules (CBMs) in lytic polysaccharide monooxygenases (LPMOs)
title On the impact of carbohydrate-binding modules (CBMs) in lytic polysaccharide monooxygenases (LPMOs)
title_full On the impact of carbohydrate-binding modules (CBMs) in lytic polysaccharide monooxygenases (LPMOs)
title_fullStr On the impact of carbohydrate-binding modules (CBMs) in lytic polysaccharide monooxygenases (LPMOs)
title_full_unstemmed On the impact of carbohydrate-binding modules (CBMs) in lytic polysaccharide monooxygenases (LPMOs)
title_short On the impact of carbohydrate-binding modules (CBMs) in lytic polysaccharide monooxygenases (LPMOs)
title_sort on the impact of carbohydrate-binding modules (cbms) in lytic polysaccharide monooxygenases (lpmos)
topic Enzymology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10154629/
https://www.ncbi.nlm.nih.gov/pubmed/36504118
http://dx.doi.org/10.1042/EBC20220162
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