Single-domain flavoenzymes trigger lytic polysaccharide monooxygenases for oxidative degradation of cellulose.
The enzymatic conversion of plant biomass has been recently revolutionized by the discovery of lytic polysaccharide monooxygenases (LPMOs) that carry out oxidative cleavage of polysaccharides. These very powerful enzymes are abundant in fungal saprotrophs. LPMOs require activation by electrons that can be provided by cellobiose dehydrogenases (CDHs), but as some fungi lack CDH-encoding genes, other recycling enzymes must exist. We investigated the ability of AA3_2 flavoenzymes secreted under lignocellulolytic conditions to trigger oxidative cellulose degradation by AA9 LPMOs. Among the flavoenzymes tested, we show that glucose dehydrogenase and aryl-alcohol quinone oxidoreductases are catalytically efficient electron donors for LPMOs. These single-domain flavoenzymes display redox potentials compatible with electron transfer between partners. Our findings extend the array of enzymes which regulate the oxidative degradation of cellulose by lignocellulolytic fungi.
INRA, Aix-Marseille Université, Polytech Marseille, UMR1163 Biodiversité et Biotechnologie Fongiques, Avenue de Luminy, F-13288 Marseille, France.|Institute of Chemistry, Slovak Academy of Sciences, Dúbravská cesta 9, 84538 Bratislava, Slovakia.
Sona
S
Garajova
INRA, Aix-Marseille Université, Polytech Marseille, UMR1163 Biodiversité et Biotechnologie Fongiques, Avenue de Luminy, F-13288 Marseille, France.
Yann
Y
Mathieu
Aix-Marseille Université, CNRS, UMR7281 Unité de Bioénergétique et Ingénierie des Protéines, F-13402 Marseille, France.
Maria Rosa
MR
Beccia
INRA, Aix-Marseille Université, Polytech Marseille, UMR1163 Biodiversité et Biotechnologie Fongiques, Avenue de Luminy, F-13288 Marseille, France.
Chloé
C
Bennati-Granier
Aix-Marseille Université, CNRS, UMR7281 Unité de Bioénergétique et Ingénierie des Protéines, F-13402 Marseille, France.
Frédéric
F
Biaso
INRA, Plateforme BIBS, Unité de Recherche Biopolymères, Interactions, Assemblages, F-44316 Nantes, France.
Mathieu
M
Fanuel
INRA, Plateforme BIBS, Unité de Recherche Biopolymères, Interactions, Assemblages, F-44316 Nantes, France.
David
D
Ropartz
Aix-Marseille Université, CNRS, UMR7281 Unité de Bioénergétique et Ingénierie des Protéines, F-13402 Marseille, France.
Bruno
B
Guigliarelli
INRA, Aix-Marseille Université, Polytech Marseille, UMR1163 Biodiversité et Biotechnologie Fongiques, Avenue de Luminy, F-13288 Marseille, France.
Eric
E
Record
INRA, Plateforme BIBS, Unité de Recherche Biopolymères, Interactions, Assemblages, F-44316 Nantes, France.
Hélène
H
Rogniaux
CNRS, UMR7257 Architecture et Fonction des Macromolécules Biologiques, 13288 Marseille, France.|INRA, USC1408 Architecture et Fonction des Macromolécules Biologiques, F-13288 Marseille, France.|Department of Biological Sciences, King Abdulaziz University, Jeddah, Saudi Arabia.
Bernard
B
Henrissat
INRA, Aix-Marseille Université, Polytech Marseille, UMR1163 Biodiversité et Biotechnologie Fongiques, Avenue de Luminy, F-13288 Marseille, France.
Jean-Guy
JG
Berrin
D002237:Carbohydrate Dehydrogenases / Q000737:chemistry* / Q000235:genetics; D005420:Flavoproteins / Q000737:chemistry* / Q000235:genetics; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000235:genetics; D048468:Podospora / Q000201:enzymology* / Q000235:genetics; D000072417:Protein Domains
D005420:Flavoproteins; D005656:Fungal Proteins; D006899:Mixed Function Oxygenases; D002237:Carbohydrate Dehydrogenases; C019859:cellobiose-quinone oxidoreductase