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Polysaccharide monooxygenase

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https://www.readbyqxmd.com/read/28919928/the-yeast-geotrichum-candidum-encodes-functional-lytic-polysaccharide-monooxygenases
#1
Simon Ladevèze, Mireille Haon, Ana Villares, Bernard Cathala, Sacha Grisel, Isabelle Herpoël-Gimbert, Bernard Henrissat, Jean-Guy Berrin
BACKGROUND: Lytic polysaccharide monooxygenases (LPMOs) are a class of powerful oxidative enzymes that have revolutionized our understanding of lignocellulose degradation. Fungal LPMOs of the AA9 family target cellulose and hemicelluloses. AA9 LPMO-coding genes have been identified across a wide range of fungal saprotrophs (Ascomycotina, Basidiomycotina, etc.), but so far they have not been found in more basal lineages. Recent genome analysis of the yeast Geotrichum candidum (Saccharomycotina) revealed the presence of several LPMO genes, which belong to the AA9 family...
2017: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/28900033/high-resolution-structure-of-a-lytic-polysaccharide-monooxygenase-from-hypocrea-jecorina-reveals-a-predicted-linker-as-an-integral-part-of-the-catalytic-domain
#2
Henrik Hansson, Saeid Karkehabadi, Nils Mikkelsen, Nicholai R Douglas, Steve Kim, Anna Lam, Thijs Kaper, Brad Kelemen, Katlyn K Meier, Stephen M Jones, Edward I Solomon, Mats Sandgren
For decades, the enzymes of the fungus Hypocrea jecorina have served as a model system for the breakdown of cellulose. Three-dimensional structures for almost all H. jecorina cellulose-degrading enzymes are available, except for HjLPMO9A, belonging to the AA9 family of lytic polysaccharide monooxygenases (LPMOs). These enzymes enhance the hydrolytic activity of cellulases and are essential for cost-efficient conversion of lignocellulosic biomass. Here, using structural and spectroscopic analyses, we found that native HjLPMO9A contains a catalytic domain and a family-1 carbohydrate-binding module (CBM1) connected via a linker sequence...
September 12, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28887418/expression-of-chitinases-in-listeria-monocytogenes-is-influenced-by-lmo0327-that-encodes-an-internalin-like-protein
#3
Dafni Katerina Paspaliari, Vicky Gaedt Kastbjerg, Hanne Ingmer, Magdalena Popowska, Marianne Halberg Larsen
The chitinolytic system of Listeria monocytogenes thus far comprises two chitinases, ChiA and ChiB, and a lytic polysaccharide monooxygenase, Lmo2467. The role of the system in the bacterium appears to be pleiotropic, as besides mediating hydrolysis of chitin, the second most ubiquitous carbohydrate in nature, the chitinases have been deemed important for colonization of unicellular moulds, as well as mammalian hosts. In order to identify additional components of the chitinolytic system, we screened a transposon mutant library for mutants exhibiting impaired chitin hydrolysis...
September 8, 2017: Applied and Environmental Microbiology
https://www.readbyqxmd.com/read/28884316/improving-extracellular-production-of-serratia-marcescens-lytic-polysaccharide-monooxygenase-cbp21-and-aeromonas-veronii-b565-chitinase-chi92-in-escherichia-coli-and-their-synergism
#4
Yalin Yang, Juan Li, Xuewei Liu, Xingliang Pan, Junxiu Hou, Chao Ran, Zhigang Zhou
Lytic polysaccharide monooxygenases (LPMOs) can oxidize recalcitrant polysaccharides and boost the conversion of the second most abundant polysaccharide chitin by chitinase. In this study, we aimed to achieve the efficient extracellular production of Serratia marcescens LPMO CBP21 and Aeromonas veronii B565 chitinase Chi92 by Escherichia coli. Twelve signal peptides reported with high secretion efficiency were screened to assess the extracellular production efficiency of CBP21 and Chi92, with glycine used as a medium supplement...
September 7, 2017: AMB Express
https://www.readbyqxmd.com/read/28846668/oxidative-cleavage-of-polysaccharides-by-monocopper-enzymes-depends-on-h2o2
#5
Bastien Bissaro, Åsmund K Røhr, Gerdt Müller, Piotr Chylenski, Morten Skaugen, Zarah Forsberg, Svein J Horn, Gustav Vaaje-Kolstad, Vincent G H Eijsink
Enzymes currently known as lytic polysaccharide monooxygenases (LPMOs) play an important role in the conversion of recalcitrant polysaccharides, but their mode of action has remained largely enigmatic. It is generally believed that catalysis by LPMOs requires molecular oxygen and a reductant that delivers two electrons per catalytic cycle. Using enzyme assays, mass spectrometry and experiments with labeled oxygen atoms, we show here that H2O2, rather than O2, is the preferred co-substrate of LPMOs. By controlling H2O2 supply, stable reaction kinetics are achieved, the LPMOs work in the absence of O2, and the reductant is consumed in priming rather than in stoichiometric amounts...
October 2017: Nature Chemical Biology
https://www.readbyqxmd.com/read/28827309/withdrawn-identification-of-an-endogenous-redox-partner-for-lytic-polysaccharide-monooxygenase-based-oxidative-cleavage-of-polysaccharides
#6
Nidhi Adlakha, Girish H Rajacharya, Rakesh Bhatnagar
This article has been withdrawn by the authors. Figs 4B and 6C were inappropriately presented.
August 21, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28822070/chemical-shift-assignments-for-the-apo-form-of-the-catalytic-domain-the-linker-region-and-the-carbohydrate-binding-domain-of-the-cellulose-active-lytic-polysaccharide-monooxygenase-sclpmo10c
#7
Gaston Courtade, Zarah Forsberg, Gustav Vaaje-Kolstad, Vincent G H Eijsink, Finn L Aachmann
The apo-form of the 21.4 kDa catalytic domain and the 10.7 kDa carbohydrate binding domain of the AA10 family lytic polysaccharide monooxygenase ScLPMO10C from Streptomyces coelicolor have been isotopically labeled and recombinantly expressed in Escherichia coli. In this paper, we report the (1)H, (13)C, and (15)N chemical shift assignments of each individual domain as well as an ensemble of the assignment for the full-length protein, including its approximately 30-amino acid long linker.
August 18, 2017: Biomolecular NMR Assignments
https://www.readbyqxmd.com/read/28750348/a-comparative-study-on-the-activity-of-fungal-lytic-polysaccharide-monooxygenases-for-the-depolymerization-of-cellulose-in-soybean-spent-flakes
#8
Brian C Pierce, Jane Wittrup Agger, Zhenghong Zhang, Jesper Wichmann, Anne S Meyer
Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes capable of the oxidative breakdown of polysaccharides. They are of industrial interest due to their ability to enhance the enzymatic depolymerization of recalcitrant substrates by glycoside hydrolases. In this paper, twenty-four lytic polysaccharide monooxygenases (LPMOs) expressed in Trichoderma reesei were evaluated for their ability to oxidize the complex polysaccharides in soybean spent flakes, an abundant and industrially relevant substrate...
September 8, 2017: Carbohydrate Research
https://www.readbyqxmd.com/read/28712648/elucidating-biochemical-features-and-biological-roles-of-streptomyces-proteins-recognizing-crystalline-chitin-and-cellulose-types-and-their-soluble-derivatives
#9
Hildgund Schrempf
Pioneering biochemical, immunological, physiological and microscopic studies in combination with gene cloning allowed uncovering previously unknown genes encoding proteins of streptomycetes to target crystalline chitin and cellulose as well as their soluble degradation-compounds via binding protein dependent transporters. Complementary analyses provoked an understanding of novel regulators governing transcription of selected genes. These discoveries induced detecting close and distant homologues of former orphan proteins encoded by genes from different bacteria...
June 20, 2017: Carbohydrate Research
https://www.readbyqxmd.com/read/28702082/enzymatic-degradation-of-sulfite-pulped-softwoods-and-the-role-of-lpmos
#10
Piotr Chylenski, Dejan M Petrović, Gerdt Müller, Marie Dahlström, Oskar Bengtsson, Martin Lersch, Matti Siika-Aho, Svein Jarle Horn, Vincent G H Eijsink
BACKGROUND: Recent advances in the development of enzyme cocktails for degradation of lignocellulosic biomass, especially the discovery of lytic polysaccharide monooxygenases (LPMOs), have opened new perspectives for process design and optimization. Softwood biomass is an abundant resource in many parts of the world, including Scandinavia, but efficient pretreatment and subsequent enzymatic hydrolysis of softwoods are challenging. Sulfite pulping-based pretreatments, such as in the BALI™ process, yield substrates that are relatively easy to degrade...
2017: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/28698982/targeting-the-reactive-intermediate-in-polysaccharide-monooxygenases
#11
Erik D Hedegård, Ulf Ryde
Lytic polysaccharide monooxygenases (LPMOs) are copper metalloenzymes that can enhance polysaccharide depolymerization through an oxidative mechanism, making them interesting for the production of biofuel from cellulose. However, the details of this activation are unknown; in particular, the nature of the intermediate that attacks the glycoside C-H bond in the polysaccharide is not known, and a number of different species have been suggested. The homolytic bond-dissociation energy (BDE) has often been used as a descriptor for the bond-activation power, especially for inorganic model complexes...
July 11, 2017: Journal of Biological Inorganic Chemistry: JBIC
https://www.readbyqxmd.com/read/28659491/physiological-and-molecular-understanding-of-bacterial-polysaccharide-monooxygenases
#12
REVIEW
Marco Agostoni, John A Hangasky, Michael A Marletta
Bacteria have long been known to secrete enzymes that degrade cellulose and chitin. The degradation of these two polymers predominantly involves two enzyme families that work synergistically with one another: glycoside hydrolases (GHs) and polysaccharide monooxygenases (PMOs). Although bacterial PMOs are a relatively recent addition to the known biopolymer degradation machinery, there is an extensive amount of literature implicating PMO in numerous physiological roles. This review focuses on these diverse and physiological aspects of bacterial PMOs, including facilitating endosymbiosis, conferring a nutritional advantage, and enhancing virulence in pathogenic organisms...
September 2017: Microbiology and Molecular Biology Reviews: MMBR
https://www.readbyqxmd.com/read/28624475/oxidoreductases-on-their-way-to-industrial-biotransformations
#13
REVIEW
Angel T Martínez, Francisco J Ruiz-Dueñas, Susana Camarero, Ana Serrano, Dolores Linde, Henrik Lund, Jesper Vind, Morten Tovborg, Owik M Herold-Majumdar, Martin Hofrichter, Christiane Liers, René Ullrich, Katrin Scheibner, Giovanni Sannia, Alessandra Piscitelli, Cinzia Pezzella, Mehmet E Sener, Sibel Kılıç, Willem J H van Berkel, Victor Guallar, Maria Fátima Lucas, Ralf Zuhse, Roland Ludwig, Frank Hollmann, Elena Fernández-Fueyo, Eric Record, Craig B Faulds, Marta Tortajada, Ib Winckelmann, Jo-Anne Rasmussen, Mirjana Gelo-Pujic, Ana Gutiérrez, José C Del Río, Jorge Rencoret, Miguel Alcalde
Fungi produce heme-containing peroxidases and peroxygenases, flavin-containing oxidases and dehydrogenases, and different copper-containing oxidoreductases involved in the biodegradation of lignin and other recalcitrant compounds. Heme peroxidases comprise the classical ligninolytic peroxidases and the new dye-decolorizing peroxidases, while heme peroxygenases belong to a still largely unexplored superfamily of heme-thiolate proteins. Nevertheless, basidiomycete unspecific peroxygenases have the highest biotechnological interest due to their ability to catalyze a variety of regio- and stereo-selective monooxygenation reactions with H2O2 as the source of oxygen and final electron acceptor...
November 1, 2017: Biotechnology Advances
https://www.readbyqxmd.com/read/28562644/a-quantitative-indicator-diagram-for-lytic-polysaccharide-monooxygenases-reveals-the-role-of-aromatic-surface-residues-in-hjlpmo9a-regioselectivity
#14
Barbara Danneels, Magali Tanghe, Henk-Jan Joosten, Thomas Gundinger, Oliver Spadiut, Ingeborg Stals, Tom Desmet
Lytic polysaccharide monooxygenases (LPMOs) have changed our understanding of lignocellulosic degradation dramatically over the last years. These metalloproteins catalyze oxidative cleavage of recalcitrant polysaccharides and can act on the C1 and/or C4 position of glycosidic bonds. Structural data have led to several hypotheses, but we are still a long way from reaching complete understanding of the factors that determine their divergent regioselectivity. Site-directed mutagenesis enables the investigation of structure-function relationship in enzymes and will be of major importance in unraveling this intriguing matter...
2017: PloS One
https://www.readbyqxmd.com/read/28535872/fungal-secretomics-to-probe-the-biological-functions-of-lytic-polysaccharide-monooxygenases
#15
Jean-Guy Berrin, Marie-Noëlle Rosso, Maher Abou Hachem
Enzymatic degradation of plant biomass is of growing interest for the development of a sustainable bio-based industry. Filamentous fungi, which degrade complex and recalcitrant plant polymers, are proficient secretors of enzymes acting on the lignocellulose composite of plant cell walls in addition to starch, the main carbon storage reservoir. In this review, we focus on the identification of lytic polysaccharide monooxygenases (LPMOs) and their redox partners in fungal secretomes to highlight the biological functions of these remarkable enzyme systems and we discuss future trends related to LPMO-potentiated bioconversion...
May 17, 2017: Carbohydrate Research
https://www.readbyqxmd.com/read/28515785/recombinant-expression-of-thermostable-processive-mteg5-endoglucanase-and-its-synergism-with-mtlpmo-from-myceliophthora-thermophila-during-the-hydrolysis-of-lignocellulosic-substrates
#16
Anthi Karnaouri, Madhu Nair Muraleedharan, Maria Dimarogona, Evangelos Topakas, Ulrika Rova, Mats Sandgren, Paul Christakopoulos
BACKGROUND: Filamentous fungi are among the most powerful cellulolytic organisms in terrestrial ecosystems. To perform the degradation of lignocellulosic substrates, these microorganisms employ both hydrolytic and oxidative mechanisms that involve the secretion and synergism of a wide variety of enzymes. Interactions between these enzymes occur on the level of saccharification, i.e., the release of neutral and oxidized products, but sometimes also reflected in the substrate liquefaction...
2017: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/28496100/structure-and-function-of-a-broad-specificity-chitin-deacetylase-from-aspergillus-nidulans-fgsc-a4
#17
Zhanliang Liu, Laurie M Gay, Tina R Tuveng, Jane W Agger, Bjørge Westereng, Geir Mathiesen, Svein J Horn, Gustav Vaaje-Kolstad, Daan M F van Aalten, Vincent G H Eijsink
Enzymatic conversion of chitin, a β-1,4 linked polymer of N-acetylglucosamine, is of major interest in areas varying from the biorefining of chitin-rich waste streams to understanding how medically relevant fungi remodel their chitin-containing cell walls. Although numerous chitinolytic enzymes have been studied in detail, relatively little is known about enzymes capable of deacetylating chitin. We describe the structural and functional characterization of a 237 residue deacetylase (AnCDA) from Aspergillus nidulans FGSC A4...
May 11, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28491137/boosting-lpmo-driven-lignocellulose-degradation-by-polyphenol-oxidase-activated-lignin-building-blocks
#18
Matthias Frommhagen, Sumanth Kumar Mutte, Adrie H Westphal, Martijn J Koetsier, Sandra W A Hinz, Jaap Visser, Jean-Paul Vincken, Dolf Weijers, Willem J H van Berkel, Harry Gruppen, Mirjam A Kabel
BACKGROUND: Many fungi boost the deconstruction of lignocellulosic plant biomass via oxidation using lytic polysaccharide monooxygenases (LPMOs). The application of LPMOs is expected to contribute to ecologically friendly conversion of biomass into fuels and chemicals. Moreover, applications of LPMO-modified cellulose-based products may be envisaged within the food or material industry. RESULTS: Here, we show an up to 75-fold improvement in LPMO-driven cellulose degradation using polyphenol oxidase-activated lignin building blocks...
2017: Biotechnology for Biofuels
https://www.readbyqxmd.com/read/28481095/neutron-and-atomic-resolution-x-ray-structures-of-a-lytic-polysaccharide-monooxygenase-reveal-copper-mediated-dioxygen-binding-and-evidence-for-n-terminal-deprotonation
#19
John-Paul Bacik, Sophanit Mekasha, Zarah Forsberg, Andrey Y Kovalevsky, Gustav Vaaje-Kolstad, Vincent G H Eijsink, Jay C Nix, Leighton Coates, Matthew J Cuneo, Clifford J Unkefer, Julian C-H Chen
A 1.1 Å resolution, room-temperature X-ray structure and a 2.1 Å resolution neutron structure of a chitin-degrading lytic polysaccharide monooxygenase domain from the bacterium Jonesia denitrificans (JdLPMO10A) show a putative dioxygen species equatorially bound to the active site copper. Both structures show an elongated density for the dioxygen, most consistent with a Cu(II)-bound peroxide. The coordination environment is consistent with Cu(II). In the neutron and X-ray structures, difference maps reveal the N-terminal amino group, involved in copper coordination, is present as a mixed ND2 and ND(-), suggesting a role for the copper ion in shifting the pKa of the amino terminus...
May 23, 2017: Biochemistry
https://www.readbyqxmd.com/read/28450248/fungal-lytic-polysaccharide-monooxygenases-from-family-aa9-recent-developments-and-application-in-lignocelullose-breakdown
#20
REVIEW
Antonielle Vieira Monclaro, Edivaldo Ximenes Ferreira Filho
Fungal lytic polysaccharide monooxygenases (LPMOs) from family AA9 are oxidative enzymes that, in the past few years, have changed the paradigm of cellulose conversion. They are key factor in the lignocellulose breakdown and are widely distributed among fungi. This review focuses on LPMOs from family AA9 and gives an overview of recent discoveries relative to their structure, mode of action, and synergism with other enzymes. Finally, several aspects regarding their potential applications toward deconstruction of biomass and biorefinery processes are discussed...
September 2017: International Journal of Biological Macromolecules
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