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https://www.readbyqxmd.com/read/29901989/multi-point-precision-binding-of-substrate-protects-lpmos-from-self-destructive-off-pathway-processes
#1
Jennifer Sarah Maria Loose, Magnus Øverlie Arntzen, Bastien Bissaro, Roland Ludwig, Vincent G H Eijsink, Gustav Vaaje-Kolstad
Lytic polysaccharide monooxygenases (LPMOs) play a crucial role in the degradation of polysaccharides in biomass by catalyzing powerful oxidative chemistry using only a single copper ion as co-factor. Despite the natural abundance and importance of these powerful mono-copper enzymes, the structural determinants of their functionality have remained largely unknown. We have used site-directed mutagenesis to probe the roles of 13 conserved amino acids located on the flat substrate-binding surface of CBP21, a chitin-active family AA10 LPMO from Serratia marcescens, also known as SmLPMO10A...
June 14, 2018: Biochemistry
https://www.readbyqxmd.com/read/29896168/distinct-substrate-specificities-and-electron-donating-systems-of-fungal-lytic-polysaccharide-monooxygenases
#2
REVIEW
Matthias Frommhagen, Adrie H Westphal, Willem J H van Berkel, Mirjam A Kabel
Lytic polysaccharide monooxygenases (LPMOs) are powerful enzymes that oxidatively cleave glycosidic bonds in polysaccharides. The ability of these copper enzymes to boost the degradation of lignocellulose has greatly stimulated research efforts and biocatalytic applications within the biorefinery field. Initially found as oxidizing recalcitrant substrates, such as chitin and cellulose, it is now clear that LPMOs cleave a broad range of oligo- and poly-saccharides and make use of various electron-donating systems...
2018: Frontiers in Microbiology
https://www.readbyqxmd.com/read/29780519/molecular-mechanism-of-lytic-polysaccharide-monooxygenases
#3
Erik Donovan Hedegård, Ulf Ryde
The lytic polysaccharide monooxygenases (LPMOs) are copper metalloenzymes that can enhance polysaccharide depolymerization through an oxidative mechanism and hence boost generation of biofuel from e.g. cellulose. By employing density functional theory in a combination of quantum mechanics and molecular mechanics (QM/MM), we report a complete description of the molecular mechanism of LPMOs. The QM/MM scheme allows us to describe all reaction steps with a detailed protein environment and we show that this is necessary...
April 21, 2018: Chemical Science
https://www.readbyqxmd.com/read/29660793/structural-and-molecular-dynamics-studies-of-a-c1-oxidizing-lytic-polysaccharide-monooxygenase-from-heterobasidion-irregulare-reveal-amino-acids-important-for-substrate-recognition
#4
Bing Liu, Abhishek A Kognole, Miao Wu, Bjørge Westereng, Michael F Crowley, Seonah Kim, Maria Dimarogona, Christina M Payne, Mats Sandgren
Lytic polysaccharide monooxygenases (LPMOs) are a group of recently discovered enzymes that play important roles in the decomposition of recalcitrant polysaccharides. Here, we report the biochemical, structural, and computational characterization of an LPMO from the white-rot fungus Heterobasidion irregulare (HiLPMO9B). This enzyme oxidizes cellulose at the C1 carbon of glycosidic linkages. The crystal structure of HiLPMO9B was determined at 2.1 Å resolution using X-ray crystallography. Unlike the majority of the currently available C1-specific LPMO structures, the HiLPMO9B structure contains an extended L2 loop, connecting β-strands β2 and β3 of the β-sandwich structure...
April 16, 2018: FEBS Journal
https://www.readbyqxmd.com/read/29614953/transcriptome-and-secretome-analysis-of-aspergillus-fumigatus-in-the-presence-of-sugarcane-bagasse
#5
Paula Fagundes de Gouvêa, Aline Vianna Bernardi, Luis Eduardo Gerolamo, Emerson de Souza Santos, Diego Mauricio Riaño-Pachón, Sergio Akira Uyemura, Taisa Magnani Dinamarco
BACKGROUND: Sugarcane bagasse has been proposed as a lignocellulosic residue for second-generation ethanol (2G) produced by breaking down biomass into fermentable sugars. The enzymatic cocktails for biomass degradation are mostly produced by fungi, but low cost and high efficiency can consolidate 2G technologies. A. fumigatus plays an important role in plant biomass degradation capabilities and recycling. To gain more insight into the divergence in gene expression during steam-exploded bagasse (SEB) breakdown, this study profiled the transcriptome of A...
April 3, 2018: BMC Genomics
https://www.readbyqxmd.com/read/29602785/the-pyrroloquinoline-quinone-dependent-pyranose-dehydrogenase-from-coprinopsis-cinerea-cc-pdh-drives-lytic-polysaccharide-monooxygenase-lpmo-action
#6
Anikó Várnai, Kiwamu Umezawa, Makoto Yoshida, Vincent G H Eijsink
Fungi secrete a set of glycoside hydrolases and oxidoreductases, including lytic polysaccharide monooxygenases (LPMOs), for the degradation of plant polysaccharides. LPMOs catalyze the oxidative cleavage of glycosidic bonds after activation by an external electron donor. So far, only flavin-dependent oxidoreductases (from the auxiliary activity family AA3) have been shown to activate LPMOs. Here we present LPMO activation by a pyrroloquinoline-quinone (PQQ)-dependent pyranose dehydrogenase (PDH) from Coprinopsis cinerea , Cc PDH, the founding member of the recently discovered auxiliary activity family AA12...
March 30, 2018: Applied and Environmental Microbiology
https://www.readbyqxmd.com/read/29588664/a-fast-and-sensitive-activity-assay-for-lytic-polysaccharide-monooxygenase
#7
Erik Breslmayr, Marija Hanžek, Aoife Hanrahan, Christian Leitner, Roman Kittl, Božidar Šantek, Chris Oostenbrink, Roland Ludwig
Background: Lytic polysaccharide monooxygenases (LPMO) release a spectrum of cleavage products from their polymeric substrates cellulose, hemicellulose, or chitin. The correct identification and quantitation of these released products is the basis of MS/HPLC-based detection methods for LPMO activity. The duration, effort, and intricate analysis allow only specialized laboratories to measure LPMO activity in day-to-day work. A spectrophotometric assay will simplify the screening for LPMO in culture supernatants, help monitor recombinant LPMO expression and purification, and support enzyme characterization...
2018: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/29498832/how-a-lytic-polysaccharide-monooxygenase-binds-crystalline-chitin
#8
Bastien Bissaro, Ingvild Isaksen, Gustav Vaaje-Kolstad, Vincent G H Eijsink, Åsmund K Røhr
Lytic polysaccharide monooxygenases (LPMOs) are major players in biomass conversion, both in Nature and in the biorefining industry. How the monocopper LPMO active site is positioned relative to the crystalline substrate surface to catalyze powerful, but potentially self-destructive, oxidative chemistry is one of the major questions in the field. We have adopted a multidisciplinary approach, combining biochemical, spectroscopic, and molecular modeling methods to study chitin binding by the well-studied LPMO from Serratia marcescens SmAA10A (or CBP21)...
March 27, 2018: Biochemistry
https://www.readbyqxmd.com/read/29472725/an-ancient-family-of-lytic-polysaccharide-monooxygenases-with-roles-in-arthropod-development-and-biomass-digestion
#9
Federico Sabbadin, Glyn R Hemsworth, Luisa Ciano, Bernard Henrissat, Paul Dupree, Theodora Tryfona, Rita D S Marques, Sean T Sweeney, Katrin Besser, Luisa Elias, Giovanna Pesante, Yi Li, Adam A Dowle, Rachel Bates, Leonardo D Gomez, Rachael Simister, Gideon J Davies, Paul H Walton, Neil C Bruce, Simon J McQueen-Mason
Thermobia domestica belongs to an ancient group of insects and has a remarkable ability to digest crystalline cellulose without microbial assistance. By investigating the digestive proteome of Thermobia, we have identified over 20 members of an uncharacterized family of lytic polysaccharide monooxygenases (LPMOs). We show that this LPMO family spans across several clades of the Tree of Life, is of ancient origin, and was recruited by early arthropods with possible roles in remodeling endogenous chitin scaffolds during development and metamorphosis...
February 22, 2018: Nature Communications
https://www.readbyqxmd.com/read/29467819/real-time-imaging-reveals-that-lytic-polysaccharide-monooxygenase-promotes-cellulase-activity-by-increasing-cellulose-accessibility
#10
Bo Song, Bingyao Li, Xiaoyan Wang, Wei Shen, Sungjin Park, Cynthia Collings, Anran Feng, Steve J Smith, Jonathan D Walton, Shi-You Ding
Background: The high cost of enzymes is one of the key technical barriers that must be overcome to realize the economical production of biofuels and biomaterials from biomass. Supplementation of enzyme cocktails with lytic polysaccharide monooxygenase (LPMO) can increase the efficiency of these cellulase mixtures for biomass conversion. The previous studies have revealed that LPMOs cleave polysaccharide chains by oxidization of the C1 and/or C4 carbons of the monomeric units. However, how LPMOs enhance enzymatic degradation of lignocellulose is still poorly understood...
2018: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/29453372/enzyme-mediated-nanofibrillation-of-cellulose-by-the-synergistic-actions-of-an-endoglucanase-lytic-polysaccharide-monooxygenase-lpmo-and-xylanase
#11
Jinguang Hu, Dong Tian, Scott Renneckar, Jack N Saddler
Physiochemical methods have generally been used to "open-up" biomass substrates/pulps and have been the main method used to fibrillate cellulose. However, recent work has shown that canonical cellulase enzymes such as endoglucanases, in combination with "amorphogenesis inducing" proteins such as lytic polysaccharide monooxygenases (LPMO), swollenin and hemicellulases, are able to increase cellulose accessibility. In the work reported here different combinations of endoglucanase, LPMO and xylanase were applied to Kraft pulps to assess their potential to induce fibrillation at low enzyme loading over a short time period...
February 16, 2018: Scientific Reports
https://www.readbyqxmd.com/read/29377002/lytic-xylan-oxidases-from-wood-decay-fungi-unlock-biomass-degradation
#12
Marie Couturier, Simon Ladevèze, Gerlind Sulzenbacher, Luisa Ciano, Mathieu Fanuel, Céline Moreau, Ana Villares, Bernard Cathala, Florence Chaspoul, Kristian E Frandsen, Aurore Labourel, Isabelle Herpoël-Gimbert, Sacha Grisel, Mireille Haon, Nicolas Lenfant, Hélène Rogniaux, David Ropartz, Gideon J Davies, Marie-Noëlle Rosso, Paul H Walton, Bernard Henrissat, Jean-Guy Berrin
Wood biomass is the most abundant feedstock envisioned for the development of modern biorefineries. However, the cost-effective conversion of this form of biomass into commodity products is limited by its resistance to enzymatic degradation. Here we describe a new family of fungal lytic polysaccharide monooxygenases (LPMOs) prevalent among white-rot and brown-rot basidiomycetes that is active on xylans-a recalcitrant polysaccharide abundant in wood biomass. Two AA14 LPMO members from the white-rot fungus Pycnoporus coccineus substantially increase the efficiency of wood saccharification through oxidative cleavage of highly refractory xylan-coated cellulose fibers...
March 2018: Nature Chemical Biology
https://www.readbyqxmd.com/read/29374564/structural-investigation-of-cellobiose-dehydrogenase-iia-insights-from-small-angle-scattering-into-intra-and-intermolecular-electron-transfer-mechanisms
#13
Annette M Bodenheimer, William B O'Dell, Ryan C Oliver, Shuo Qian, Christopher B Stanley, Flora Meilleur
BACKGROUND: Cellobiose dehydrogenases have gained interest due to their potential applications in sectors from biofuel production to biomedical devices. The CDHIIA variant is comprised of a cytochrome domain (CYT), a dehydrogenase domain (DH), and a carbohydrate-binding module (CBM) that are connected by two flexible linkers. Upon cellobiose oxidation at the DH, intramolecular electron transfer (IaET) occurs from the DH to the CYT. In vivo, CDHIIA CYT subsequently performs intermolecular electron transfer (IeET) to a lytic polysaccharide monooxygenase (LPMO)...
April 2018: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/29371886/laccase-derived-lignin-compounds-boost-cellulose-oxidative-enzymes-aa9
#14
Lívia Brenelli, Fabio M Squina, Claus Felby, David Cannella
Background: The discovery of lignin as activator for the redox enzyme lytic polysaccharide monooxygenases (LPMOs) for the oxidation of cell-wall polysaccharides opens a new scenario for investigation of the interplay between different lignocellulose-degrading enzymes. The lignin-active enzymes in one hand, and the carbohydrate active in the other, are linked through a variety of electrons carrier molecules either derived from lignin or enzymatically transferred. Likewise, in nature, many lignocellulose-degrading organisms are expressing those enzymes simultaneously, and we wanted to test if a major commercial available lignin oxidase enzyme, i...
2018: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/29259205/action-of-lytic-polysaccharide-monooxygenase-on-plant-tissue-is-governed-by-cellular-type
#15
Brigitte Chabbert, Anouck Habrant, Mickaël Herbaut, Laurence Foulon, Véronique Aguié-Béghin, Sona Garajova, Sacha Grisel, Chloé Bennati-Granier, Isabelle Gimbert-Herpoël, Frédéric Jamme, Matthieu Réfrégiers, Christophe Sandt, Jean-Guy Berrin, Gabriel Paës
Lignocellulosic biomass bioconversion is hampered by the structural and chemical complexity of the network created by cellulose, hemicellulose and lignin. Biological conversion of lignocellulose involves synergistic action of a large array of enzymes including the recently discovered lytic polysaccharide monooxygenases (LPMOs) that perform oxidative cleavage of cellulose. Using in situ imaging by synchrotron UV fluorescence, we have shown that the addition of AA9 LPMO (from Podospora anserina) to cellulases cocktail improves the progression of enzymes in delignified Miscanthus x giganteus as observed at tissular levels...
December 19, 2017: Scientific Reports
https://www.readbyqxmd.com/read/29259126/active-site-copper-reduction-promotes-substrate-binding-of-fungal-lytic-polysaccharide-monooxygenase-and-reduces-stability
#16
Daniel Kracher, Martina Andlar, Paul G Furtmüller, Roland Ludwig
Lytic polysaccharide monooxygenases (LPMOs) are a class of copper-containing enzymes that oxidatively degrade insoluble plant polysaccharides and soluble oligosaccharides. Upon reductive activation, they cleave the substrate and promote biomass degradation by hydrolytic enzymes. In this study, we employed LPMO9C from Neurospora crassa , which is active toward cellulose and soluble β-glucans, to study the enzyme-substrate interaction and thermal stability. Binding studies showed that the reduction of the mononuclear active-site copper by ascorbic acid increased the affinity and the maximum binding capacity of LPMO for cellulose...
February 2, 2018: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/29238402/expressing-accessory-proteins-in-cellulolytic-yarrowia-lipolytica-to-improve-the-conversion-yield-of-recalcitrant-cellulose
#17
Zhong-Peng Guo, Sophie Duquesne, Sophie Bozonnet, Jean-Marc Nicaud, Alain Marty, Michael Joseph O'Donohue
Background: A recently constructed cellulolytic Yarrowia lipolytica is able to grow efficiently on an industrial organosolv cellulose pulp, but shows limited ability to degrade crystalline cellulose. In this work, we have further engineered this strain, adding accessory proteins xylanase II (XYNII), lytic polysaccharide monooxygenase (LPMO), and swollenin (SWO) from Trichoderma reesei in order to enhance the degradation of recalcitrant substrate. Results: The production of EG I was enhanced using a promoter engineering strategy...
2017: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/29232119/catalytic-mechanism-of-fungal-lytic-polysaccharide-monooxygenases-investigated-by-first-principles-calculations
#18
Luca Bertini, Raffaella Breglia, Matteo Lambrughi, Piercarlo Fantucci, Luca De Gioia, Marco Borsari, Marco Sola, Carlo Augusto Bortolotti, Maurizio Bruschi
Lytic polysaccharide monooxygenases (LPMOs) are Cu-containing enzymes that facilitate the degradation of recalcitrant polysaccharides by the oxidative cleavage of glycosidic bonds. They are gaining rapidly increasing attention as key players in biomass conversion, especially for the production of second-generation biofuels. Elucidation of the detailed mechanism of the LPMO reaction is a major step toward the assessment and optimization of LPMO efficacy in industrial biotechnology, paving the way to utilization of sustainable fuel sources...
January 2, 2018: Inorganic Chemistry
https://www.readbyqxmd.com/read/29228039/biochemical-studies-of-two-lytic-polysaccharide-monooxygenases-from-the-white-rot-fungus-heterobasidion-irregulare-and-their-roles-in-lignocellulose-degradation
#19
Bing Liu, Åke Olson, Miao Wu, Anders Broberg, Mats Sandgren
Lytic polysaccharide monooxygenases (LPMO) are important redox enzymes produced by microorganisms for the degradation of recalcitrant natural polysaccharides. Heterobasidion irregulare is a white-rot phytopathogenic fungus that causes wood decay in conifers. The genome of this fungus encodes 10 putative Auxiliary Activity family 9 (AA9) LPMOs. We describe the first biochemical characterization of H. irregulare LPMOs through heterologous expression of two CBM-containing LPMOs from this fungus (HiLPMO9H, HiLPMO9I) in Pichia pastoris...
2017: PloS One
https://www.readbyqxmd.com/read/29222333/structural-determinants-of-bacterial-lytic-polysaccharide-monooxygenase-functionality
#20
Zarah Forsberg, Bastien Bissaro, Jonathan Gullesen, Bjørn Dalhus, Gustav Vaaje-Kolstad, Vincent G H Eijsink
Bacterial lytic polysaccharide monooxygenases (LPMO10s) use redox chemistry to cleave glycosidic bonds in the two foremost recalcitrant polysaccharides found in nature, namely cellulose and chitin. Analysis of correlated mutations revealed that the substrate-binding and copper-containing surface of LPMO10s composes a network of co-evolved residues and interactions, whose roles in LPMO functionality are unclear. Here, we mutated a subset of these correlated residues in a newly characterized C1/C4-oxidizing LPMO10 from Micromonospora aurantiaca ( Ma LPMO10B) to the corresponding residues in strictly C1-oxidizing LPMO10s...
January 26, 2018: Journal of Biological Chemistry
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