Abstract Bacterial proteins categorized as family 33 carbohydrate‐binding modules (CBM33) were recently shown to cleave crystalline chitin, using a mechanism that involves hydrolysis and oxidation. We show here some members of the CBM33 cellulose demonstrated by chromatographic mass spectrometric analyses soluble products released from Avicel or filter paper on incubation with CelS2, CBM33‐containing protein Streptomyces coelicolor A3(2). These enzymes act synergistically cellulases may thus...

Significance The discovery of lytic polysaccharide monooxygenases (LPMOs) has profoundly changed our understanding the enzymatic conversion recalcitrant polysaccharides, such as cellulose. Although in-depth studies fungal cellulolytic LPMOs have been reported, structures and functions their bacterial counterparts with no detectable sequence similarity remain largely elusive. We present a conserved pair cellulose-active supplemented extensive functional characterization. structural data allow...

The discovery of the copper‐dependent lytic polysaccharide monooxygenases (LPMOs) has revealed new territory for chemical and biochemical analysis. These unique mononuclear copper enzymes are abundant, suggesting functional diversity beyond their established roles in depolymerization biomass polysaccharides. At same time basic methods characterizing LPMOs, such as activity assays not well developed. Here we describe a method quantification C1‐oxidized chitooligosaccharides (aldonic acids),...

Lytic polysaccharide monooxygenases (LPMOs), found in family 9 (previously GH61), 10 CBM33), and the newly discovered 11 of auxiliary activities (AA) carbohydrate-active enzyme classification system, are copper-dependent enzymes that oxidize sp(3)-carbons recalcitrant polysaccharides such as chitin cellulose presence an external electron donor. In this study, we describe activity two AA10-type LPMOs whose have not been described before compare total four different with aim finding possible...

Cellvibrio japonicusis a Gram-negative soil bacterium that is primarily known for its ability to degrade plant cell wall polysaccharides through utilization of an extensive repertoire carbohydrate-active enzymes. Several putative chitin-degrading enzymes are also found among these enzymes, such as chitinases, chitobiases, and lytic polysaccharide monooxygenases (LPMOs). In this study, we have characterized the chitin-active LPMO,CjLPMO10A, tri-modular enzyme containing catalytic family AA10...

Abstract Background Lytic polysaccharide monooxygenases (LPMOs) are monocopper enzymes that catalyze oxidative depolymerization of industrially relevant crystalline polysaccharides, such as cellulose, in a reaction depends on an electron donor and O 2 or H . While it is well known LPMOs can utilize wide variety donors, the variation reported efficiencies various LPMO-reductant combinations remains largely unexplained. Results In this study, we describe novel two-domain cellulose-active...

Lytic polysaccharide monooxygenases (LPMOs) are mono-copper enzymes that catalyze oxidative depolymerization of recalcitrant substrates such as chitin or cellulose. Recent work has shown LPMOs fast peroxygenase reactions and that, under commonly used reaction set-ups, access to in situ generated H2O2 likely limits catalysis. Based on a hypothesis the impact cellulose-binding module (CBM) LPMO activity could relate changes production, we have assessed interplay between CBM-containing...

Abstract Lytic polysaccharide monooxygenases (LPMOs) represent a recent addition to the carbohydrate‐active enzymes and are classified as auxiliary activity (AA) families 9, 10, 11, 13. LPMOs crucial for effective degradation of recalcitrant polysaccharides like cellulose or chitin. These copper‐dependent utilize redox mechanism cleave glycosidic bonds that is dependent on molecular oxygen an external electron donor. The electrons can be provided by various sources, such chemical compounds...

Light-driven oxidation of water catalyzed by a photocatalyst can fuel the activity LPMOs, key enzymes in processing recalcitrant polysaccharides.

The catalytic function of lytic polysaccharide monooxygenases (LPMOs) to cleave and decrystallize recalcitrant polysaccharides put these enzymes in the spotlight fundamental applied research. Here we demonstrate that demand LPMO for an electron donor oxygen species as cosubstrate can be fulfilled by a single auxiliary enzyme: engineered fungal cellobiose dehydrogenase (CDH) with increased oxidase activity. CDH was about 30 times more efficient driving reaction due its 27 time production H2...

Monocopper lytic polysaccharide monooxygenases (LPMOs) catalyse oxidative cleavage of glycosidic bonds in a reductant‐dependent reaction. Recent studies indicate that LPMOs, rather than being O 2 ‐dependent monooxygenases, are H peroxygenases. Here, we describe Ssc LPMO10B, novel LPMO from the phytopathogenic bacterium Streptomyces scabies and address links between this enzyme’s catalytic rate situ hydrogen peroxide production presence ascorbic acid, gallic acid l ‐cysteine. Studies Avicel...

Microbial depolymerization of plant cell walls contributes to global carbon balance and is a critical component renewable energy. The genomes lignocellulose degrading microorganisms encode diverse classes carbohydrate modifying enzymes, although currently there paucity knowledge on the role these proteins in vivo. We report comprehensive analysis cellulose degradation system saprophytic bacterium Cellvibrio japonicus. Gene expression profiling C. japonicus demonstrated that three 12...

A 1.1 Å resolution, room-temperature X-ray structure and a 2.1 resolution neutron of chitin-degrading lytic polysaccharide monooxygenase domain from the bacterium Jonesia denitrificans (JdLPMO10A) show putative dioxygen species equatorially bound to active site copper. Both structures an elongated density for dioxygen, most consistent with Cu(II)-bound peroxide. The coordination environment is Cu(II). In structures, difference maps reveal N-terminal amino group, involved in copper...

Lytic polysaccharide monooxygenases (LPMOs) contribute to enzymatic conversion of recalcitrant polysaccharides such as chitin and cellulose may also play a role in bacterial infections. Some LPMOs are multimodular, the implications which remain only partly understood. We have studied properties tetra‐modular LPMO from food poisoning bacterium Bacillus cereus (named Bc LPMO10A). show that LPMO10A, comprising an domain, two fibronectin‐type III (FnIII)‐like domains, carbohydrate‐binding module...

Significance Lytic polysaccharide monooxygenases (LPMOs) have unique catalytic centers, at which a single copper catalyzes the oxidative cleavage of glycosidic bond. The mechanism by LPMOs activate molecular oxygen is key to understanding (bio)catalysis but remains poorly understood, largely because insoluble and heterogeneous nature LPMO substrates precludes use usual laboratory techniques. Using an integrated NMR/EPR approach, we unraveled structural electronic details interactions from...

Abstract Bacterial lytic polysaccharide monooxygenases (LPMOs) are known to oxidize the most abundant and recalcitrant polymers in Nature, namely cellulose chitin. The genome of model actinomycete Streptomyces coelicolor A3(2) encodes seven putative LPMOs, which, upon phylogenetic analysis, four group with typical chitin-oxidizing two cellulose-active one which stands out by being part a subclade non-characterized enzymes. latter enzyme, called Sc LPMO10D, enzymes found this unique, not only...