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Polysaccharide monooxygenase

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https://www.readbyqxmd.com/read/29145801/comparative-genomics-of-coniophora-olivacea-reveals-different-patterns-of-genome-expansion-in-boletales
#1
Raúl Castanera, Gúmer Pérez, Leticia López-Varas, Joëlle Amselem, Kurt LaButti, Vasanth Singan, Anna Lipzen, Sajeet Haridas, Kerrie Barry, Igor V Grigoriev, Antonio G Pisabarro, Lucía Ramírez
BACKGROUND: Coniophora olivacea is a basidiomycete fungus belonging to the order Boletales that produces brown-rot decay on dead wood of conifers. The Boletales order comprises a diverse group of species including saprotrophs and ectomycorrhizal fungi that show important differences in genome size. RESULTS: In this study we report the 39.07-megabase (Mb) draft genome assembly and annotation of C. olivacea. A total of 14,928 genes were annotated, including 470 putatively secreted proteins enriched in functions involved in lignocellulose degradation...
November 16, 2017: BMC Genomics
https://www.readbyqxmd.com/read/29138240/kinetics-of-h2o2-driven-degradation-of-chitin-by-a-bacterial-lytic-polysaccharide-monooxygenase
#2
Silja Kuusk, Bastien Bissaro, Piret Kuusk, Zarah Forsberg, Vincent G H Eijsink, Morten Sørlie, Priit Väljamäe
Lytic polysaccharide monooxygenases (LPMOs) catalyze the oxidative cleavage of glycosidic bonds in recalcitrant polysaccharides, such as cellulose and chitin, and are of interest in biotechnological utilization of these abundant biomaterials. It has recently been shown that LPMOs can use H2O2, instead of O2, as a co-substrate. This peroxygenase-like reaction by a mono-copper enzyme is unprecedented in nature and opens new avenues in chemistry and enzymology. Here, we provide the first detailed kinetic characterization of chitin degradation by the bacterial LPMO chitin-binding protein CBP21 using H2O2 as co-substrate...
November 14, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/29100178/monitoring-of-reactions-catalyzed-by-lytic-polysaccharide-monooxygenases-using-highly-sensitive-fluorimetric-assay-of-the-oxygen-consumption-rate
#3
Alexander V Gusakov, Alexander G Bulakhov, Ilya N Demin, Arkady P Sinitsyn
Lytic polysaccharide monooxygenases (LPMOs) are recently discovered enzymes that catalyze the oxidative deconstruction of polysaccharides. However fast and reliable methods of determination of LPMO activity still need to be developed, especially those based on the initial reaction rates. A method based on the oxygen consumption rate (OCR) measurements, using a Seahorse XFp Analyzer with highly-sensitive fluorimetric sensors, was applied for monitoring the oxidation of amorphous cellulose by three fungal LPMOs: recombinant enzymes from Thielavia terrestris (GH61E), Trichoderma reesei (Cel61A), and a native LPMO9A from Myceliophthora thermophila...
November 27, 2017: Carbohydrate Research
https://www.readbyqxmd.com/read/29100023/lignocellulose-deconstruction-in-the-biosphere
#4
REVIEW
Yannick J Bomble, Chien-Yuan Lin, Antonella Amore, Hui Wei, Evert K Holwerda, Peter N Ciesielski, Bryon S Donohoe, Stephen R Decker, Lee R Lynd, Michael E Himmel
Microorganisms have evolved different and yet complementary mechanisms to degrade biomass in the biosphere. The chemical biology of lignocellulose deconstruction is a complex and intricate process that appears to vary in response to specific ecosystems. These microorganisms rely on simple to complex arrangements of glycoside hydrolases to conduct most of these polysaccharide depolymerization reactions and also, as discovered more recently, oxidative mechanisms via lytic polysaccharide monooxygenases or non-enzymatic Fenton reactions which are used to enhance deconstruction...
October 31, 2017: Current Opinion in Chemical Biology
https://www.readbyqxmd.com/read/29057953/structural-and-electronic-determinants-of-lytic-polysaccharide-monooxygenase-reactivity-on-polysaccharide-substrates
#5
T J Simmons, K E H Frandsen, L Ciano, T Tryfona, N Lenfant, J C Poulsen, L F L Wilson, T Tandrup, M Tovborg, K Schnorr, K S Johansen, B Henrissat, P H Walton, L Lo Leggio, P Dupree
Lytic polysaccharide monooxygenases (LPMOs) are industrially important copper-dependent enzymes that oxidatively cleave polysaccharides. Here we present a functional and structural characterization of two closely related AA9-family LPMOs from Lentinus similis (LsAA9A) and Collariella virescens (CvAA9A). LsAA9A and CvAA9A cleave a range of polysaccharides, including cellulose, xyloglucan, mixed-linkage glucan and glucomannan. LsAA9A additionally cleaves isolated xylan substrates. The structures of CvAA9A and of LsAA9A bound to cellulosic and non-cellulosic oligosaccharides provide insight into the molecular determinants of their specificity...
October 20, 2017: Nature Communications
https://www.readbyqxmd.com/read/29026070/single-molecule-study-of-oxidative-enzymatic-deconstruction-of-cellulose
#6
Manuel Eibinger, Jürgen Sattelkow, Thomas Ganner, Harald Plank, Bernd Nidetzky
LPMO (lytic polysaccharide monooxygenase) represents a unique paradigm of cellulosic biomass degradation by an oxidative mechanism. Understanding the role of LPMO in deconstructing crystalline cellulose is fundamental to the enzyme's biological function and will help to specify the use of LPMO in biorefinery applications. Here we show with real-time atomic force microscopy that C1 and C4 oxidizing types of LPMO from Neurospora crassa (NcLPMO9F, NcLPMO9C) bind to nanocrystalline cellulose with high preference for the very same substrate surfaces that are also used by a processive cellulase (Trichoderma reesei CBH I) to move along during hydrolytic cellulose degradation...
October 12, 2017: Nature Communications
https://www.readbyqxmd.com/read/28919928/the-yeast-geotrichum-candidum-encodes-functional-lytic-polysaccharide-monooxygenases
#7
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
#8
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/chitinase-expression-in-listeria-monocytogenes-is-influenced-by-lmo0327-which-encodes-an-internalin-like-protein
#9
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 the hydrolysis of chitin, the second most ubiquitous carbohydrate in nature, the chitinases have been deemed important for the colonization of unicellular molds, as well as mammalian hosts. To identify additional components of the chitinolytic system, we screened a transposon mutant library for mutants exhibiting impaired chitin hydrolysis...
November 15, 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
#10
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
#11
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
#12
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
#13
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.
October 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
#14
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
#15
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
#16
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
#17
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...
October 2017: Journal of Biological Inorganic Chemistry: JBIC
https://www.readbyqxmd.com/read/28659491/physiological-and-molecular-understanding-of-bacterial-polysaccharide-monooxygenases
#18
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
#19
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
#20
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
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