ArticleThe Journal of biological chemistry2016
Structural and Functional Analysis of a Lytic Polysaccharide Monooxygenase Important for Efficient Utilization of Chitin in Cellvibrio japonicus.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 144 citations in OpenAlex.
- Reduced Processivity in a Chitobiohydrolase Enhances LPMO-Assisted Chitin Depolymerization.Biochemistry · 2026Article
- Functional Characterization of Multidomain LPMOs from MarineBiochemistry · 2026Article
- Microbial chitinases in the plant holobiont: ecological roles and structural determinants.FEMS microbiology reviews · 2026Review
- The physiological functions of the Cbp2D and Cbp2E proteins are important for insoluble cellulose-dependent growth inApplied and environmental microbiology · 2025Article
- Functional variation among LPMOs revealed by the inhibitory effects of cyanide and buffer ions.FEBS letters · 2025Article
- SGBP-B-like bimodular cellulose-binding protein CHU_1279 is essential for cellulose utilization byApplied and environmental microbiology · 2025Article
- A modular enzyme with combined hemicellulose-removing and LPMO activity increases cellulose accessibility in softwood.The FEBS journal · 2025Article
- Transcriptomic analyses of bacterial growth on fungal necromass reveal different microbial community niches during degradation.Applied and environmental microbiology · 2024Article
- Low salinity stress increases the risk of Vibrio parahaemolyticus infection and gut microbiota dysbiosis in Pacific white shrimp.BMC microbiology · 2024Article
- Heterologous Expression and Biochemical Characterization of a Novel Lytic Polysaccharide Monooxygenase fromMicroorganisms · 2024Article
- Role of Natural Binding Proteins in Therapy and Diagnostics.Life (Basel, Switzerland) · 2024Article
- Microbe Profile:Microbiology (Reading, England) · 2024Article
- The disordered C-terminal tail of fungal LPMOs from phytopathogens mediates protein dimerization and impacts plant penetration.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
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- Chitinolytic and Fungicidal Potential of the Marine Bacterial Strains Habituating Pacific Ocean Regions.Microorganisms · 2023Article
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- Isolation, biochemical characterization, and genome sequencing of two high-quality genomes of a novel chitinolytic Jeongeupia species.MicrobiologyOpen · 2023Article
- On the impact of carbohydrate-binding modules (CBMs) in lytic polysaccharide monooxygenases (LPMOs).Essays in biochemistry · 2023Review
- Structural and functional characterization of the catalytic domain of a cell-wall anchored bacterial lytic polysaccharide monooxygenase from Streptomyces coelicolor.Scientific reports · 2023Article
- Article
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
Abstract
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 of carbohydrate-active enzymes. Several putative chitin-degrading enzymes are also found among these carbohydrate-active enzymes, such as chitinases, chitobiases, and lytic polysaccharide monooxygenases (LPMOs). In this study, we have characterized the chitin-active LPMO,CjLPMO10A, a tri-modular enzyme containing a catalytic family AA10 LPMO module, a family 5 chitin-binding module, and a C-terminal unclassified module of unknown function. Characterization of the latter module revealed tight and specific binding to chitin, thereby unraveling a new family of chitin-binding modules (classified as CBM73). X-ray crystallographic elucidation of theCjLPMO10A catalytic module revealed that the active site of the enzyme combines structural features previously only observed in either cellulose or chitin-active LPMO10s. Analysis of the copper-binding site by EPR showed a signal signature more similar to those observed for cellulose-cleaving LPMOs. The full-length LPMO shows no activity toward cellulose but is able to bind and cleave both α- and β-chitin. Removal of the chitin-binding modules reduced LPMO activity toward α-chitin compared with the full-length enzyme. Interestingly, the full-length enzyme and the individual catalytic LPMO module boosted the activity of an endochitinase equally well, also yielding similar amounts of oxidized products. Finally, gene deletion studies show thatCjLPMO10A is needed byC. japonicusto obtain efficient growth on both purified chitin and crab shell particles.
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