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Single-domain flavoenzymes trigger lytic polysaccharide monooxygenases for oxidative degradation of cellulose
by
Bennati-Granier, Chloé
, Henrissat, Bernard
, Biaso, Frédéric
, Rogniaux, Hélène
, Fanuel, Mathieu
, Garajova, Sona
, Guigliarelli, Bruno
, Beccia, Maria Rosa
, Record, Eric
, Mathieu, Yann
, Ropartz, David
, Berrin, Jean-Guy
in
631/326/193/2538
/ 631/45/607/1168
/ 82/58
/ 82/80
/ Alcohol
/ Carbohydrate Dehydrogenases - chemistry
/ Carbohydrate Dehydrogenases - genetics
/ Cellulose
/ Chemical Sciences
/ Cooperation
/ Cytochrome
/ Dehydrogenases
/ Enzymes
/ Flavoproteins - chemistry
/ Flavoproteins - genetics
/ Fungal Proteins - chemistry
/ Fungal Proteins - genetics
/ Fungi
/ Humanities and Social Sciences
/ Lignin
/ Mass spectrometry
/ Mixed Function Oxygenases - chemistry
/ Mixed Function Oxygenases - genetics
/ multidisciplinary
/ Plant biomass
/ Podospora - enzymology
/ Podospora - genetics
/ Polymers
/ Protein Domains
/ Saccharides
/ Science
/ Scientific imaging
2016
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Single-domain flavoenzymes trigger lytic polysaccharide monooxygenases for oxidative degradation of cellulose
by
Bennati-Granier, Chloé
, Henrissat, Bernard
, Biaso, Frédéric
, Rogniaux, Hélène
, Fanuel, Mathieu
, Garajova, Sona
, Guigliarelli, Bruno
, Beccia, Maria Rosa
, Record, Eric
, Mathieu, Yann
, Ropartz, David
, Berrin, Jean-Guy
in
631/326/193/2538
/ 631/45/607/1168
/ 82/58
/ 82/80
/ Alcohol
/ Carbohydrate Dehydrogenases - chemistry
/ Carbohydrate Dehydrogenases - genetics
/ Cellulose
/ Chemical Sciences
/ Cooperation
/ Cytochrome
/ Dehydrogenases
/ Enzymes
/ Flavoproteins - chemistry
/ Flavoproteins - genetics
/ Fungal Proteins - chemistry
/ Fungal Proteins - genetics
/ Fungi
/ Humanities and Social Sciences
/ Lignin
/ Mass spectrometry
/ Mixed Function Oxygenases - chemistry
/ Mixed Function Oxygenases - genetics
/ multidisciplinary
/ Plant biomass
/ Podospora - enzymology
/ Podospora - genetics
/ Polymers
/ Protein Domains
/ Saccharides
/ Science
/ Scientific imaging
2016
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While trying to remove the title from your shelf something went wrong :( Kindly try again later!
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Single-domain flavoenzymes trigger lytic polysaccharide monooxygenases for oxidative degradation of cellulose
by
Bennati-Granier, Chloé
, Henrissat, Bernard
, Biaso, Frédéric
, Rogniaux, Hélène
, Fanuel, Mathieu
, Garajova, Sona
, Guigliarelli, Bruno
, Beccia, Maria Rosa
, Record, Eric
, Mathieu, Yann
, Ropartz, David
, Berrin, Jean-Guy
in
631/326/193/2538
/ 631/45/607/1168
/ 82/58
/ 82/80
/ Alcohol
/ Carbohydrate Dehydrogenases - chemistry
/ Carbohydrate Dehydrogenases - genetics
/ Cellulose
/ Chemical Sciences
/ Cooperation
/ Cytochrome
/ Dehydrogenases
/ Enzymes
/ Flavoproteins - chemistry
/ Flavoproteins - genetics
/ Fungal Proteins - chemistry
/ Fungal Proteins - genetics
/ Fungi
/ Humanities and Social Sciences
/ Lignin
/ Mass spectrometry
/ Mixed Function Oxygenases - chemistry
/ Mixed Function Oxygenases - genetics
/ multidisciplinary
/ Plant biomass
/ Podospora - enzymology
/ Podospora - genetics
/ Polymers
/ Protein Domains
/ Saccharides
/ Science
/ Scientific imaging
2016
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Single-domain flavoenzymes trigger lytic polysaccharide monooxygenases for oxidative degradation of cellulose
Journal Article
Single-domain flavoenzymes trigger lytic polysaccharide monooxygenases for oxidative degradation of cellulose
2016
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Overview
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.
Publisher
Nature Publishing Group UK,Nature Publishing Group
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