Journal Article

Discovery of fungal oligosaccharide-oxidising flavo-enzymes with previously unknown substrates, redox-activity profiles and interplay with LPMOs

Vuong, Thu, Biaso, Frédéric, Architecture et fonction des macromolécules biologiques (AFMB) ; Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Haddad Momeni, Majid, Haon, Mireille, Danmarks Tekniske Universitet = Technical University of Denmark (DTU), Fredslund, Folmer, Nielsen, Tine Sofie, Bissaro, Bastien, University of Toronto, Berrin, Jean-Guy, Welner, Ditte Hededam, Raji, Olanrewaju, Bioénergétique et Ingénierie des Protéines (BIP) ; Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Novo Nordisk Foundation Center for Biosustainability ; Danmarks Tekniske Universitet = Technical University of Denmark (DTU), Henrissat, Bernard, Grisel, Sacha, Abou Hachem, Maher, Biodiversité et Biotechnologie Fongiques (BBF) ; Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (

2021

Overview

Abstract Oxidative plant cell-wall processing enzymes are of great importance in biology and biotechnology. Yet, our insight into the functional interplay amongst such oxidative enzymes remains limited. Here, a phylogenetic analysis of the auxiliary activity 7 family (AA7), currently harbouring oligosaccharide flavo-oxidases, reveals a striking abundance of AA7-genes in phytopathogenic fungi and Oomycetes. Expression of five fungal enzymes, including three from unexplored clades, expands the AA7-substrate range and unveils a cellooligosaccharide dehydrogenase activity, previously unknown within AA7. Sequence and structural analyses identify unique signatures distinguishing the strict dehydrogenase clade from canonical AA7 oxidases. The discovered dehydrogenase directly is able to transfer electrons to an AA9 lytic polysaccharide monooxygenase (LPMO) and fuel cellulose degradation by LPMOs without exogenous reductants. The expansion of redox-profiles and substrate range highlights the functional diversity within AA7 and sets the stage for harnessing AA7 dehydrogenases to fine-tune LPMO activity in biotechnological conversion of plant feedstocks.

• Publisher: Nature Publishing Group,CCSD,Nature Publishing Group UK,Nature Portfolio
• Subject: 101/6 / 631/326/193 / 631/45/603 / 631/45/607/1168 / 631/45/72/1205 / 631/535/1266 / 82/80 / 82/83 / Biodegradation / Biodiversity and Ecology / Biotechnology / Cell Wall - chemistry / Cell Wall - metabolism / Cellooligosaccharides / Cellulose / Cellulose - metabolism / Chemical Sciences / Computer Science / Cristallography / Crystallography, X-Ray / Dehydrogenase / Dehydrogenases / DNA, Fungal - genetics / DNA, Fungal - isolation & purification / Electron-Transferring Flavoproteins - metabolism / Environmental Sciences / Enzyme Assays / Enzymes / Fuels / Fungal Proteins - genetics / Fungal Proteins - isolation & purification / Fungal Proteins - metabolism / Fungal Proteins - ultrastructure / Fungi / Humanities and Social Sciences / Industrial Microbiology - methods / Magnetic Resonance Spectroscopy / Microorganisms / Monooxygenase / multidisciplinary / Oligosaccharides / Oomycetes - enzymology / Oomycetes - genetics / Oxidation-Reduction / Oxidoreductases - genetics / Oxidoreductases - isolation & purification / Oxidoreductases - metabolism / Oxidoreductases - ultrastructure / Phylogeny / Phytopathogenic fungi / Polysaccharides / Reducing agents / Science / Science (multidisciplinary) / Sequence Analysis, DNA / Substrate Specificity / Substrates
• ISBN: 0006835446000