ArticleThe Journal of biological chemistry2015
Structural and Functional Characterization of a Lytic Polysaccharide Monooxygenase with Broad Substrate Specificity.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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Who cites it
91 citing papers in PubMed.
- Plant Biomass Depolymerization by Oxidoreductases: Structural Characteristics, Synergy Mechanism, and Evolutionary Adaptation.Journal of agricultural and food chemistry · 2026Review
- Computer-Aided Virtual Saturation Mutagenesis Improves the Lignocellulose-Degrading Performance of anFoods (Basel, Switzerland) · 2026Article
- Ligand Radicals Tune LPMO Activity in Model Complex.Inorganic chemistry · 2026Article
- Enhanced Oxidative Degradation of β-O-4 Lignin Model Compound Using Robust Lytic Polysaccharide Monooxygenase-Cobalt Phosphate Hybrid Nanoflowers.Applied biochemistry and biotechnology · 2026Article
- Electrochemical Insight into the Copper Redox Chemistry and HACS electrochemistry · 2026Article
- Structural and electronic modulations of lytic polysaccharide monooxygenase (LPMO) upon chitin binding: insights from X-ray spectroscopy.Chemical science · 2025Article
- A Molecular Mechanism for the Reduction of the Cu Site in Lytic Polysaccharide Monooxygenases by Phenol Reductants.JACS Au · 2025Article
- Anions and citrate inhibit LsAA9A, a lytic polysaccharide monooxygenase (LPMO).The FEBS journal · 2025Article
- Functional variation among LPMOs revealed by the inhibitory effects of cyanide and buffer ions.FEBS letters · 2025Article
- The impact of the carbohydrate-binding module on how a lytic polysaccharide monooxygenase modifies cellulose fibers.Biotechnology for biofuels and bioproducts · 2024Article
- Beyond the Surface: A Methodological Exploration of Enzyme Impact along the Cellulose Fiber Cross-Section.Biomacromolecules · 2024Article
- Structural dissection of two redox proteins from the shipworm symbiont Teredinibacter turnerae.IUCrJ · 2024Article
- Expanding the catalytic landscape of metalloenzymes with lytic polysaccharide monooxygenases.Nature reviews. Chemistry · 2024Review
- Assessing the role of redox partners in TthLPMO9G and its mutants: focus on HBiotechnology for biofuels and bioproducts · 2024Article
- Carbohydrate-binding modules enhance HThe Journal of biological chemistry · 2024Article
- Article
- Functional characterization of a lytic polysaccharide monooxygenase from Schizophyllum commune that degrades non-crystalline substrates.Scientific reports · 2023Article
- Functional characterization of fungal lytic polysaccharide monooxygenases for cellulose surface oxidation.Biotechnology for biofuels and bioproducts · 2023Article
- A Conserved Second Sphere Residue Tunes Copper Site Reactivity in Lytic Polysaccharide Monooxygenases.Journal of the American Chemical Society · 2023Article
- The Role of the Residue at Position 2 in the Catalytic Activity of AA9 Lytic Polysaccharide Monooxygenases.International journal of molecular sciences · 2023Article
31 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The recently discovered lytic polysaccharide monooxygenases (LPMOs) carry out oxidative cleavage of polysaccharides and are of major importance for efficient processing of biomass. NcLPMO9C from Neurospora crassa acts both on cellulose and on non-cellulose β-glucans, including cellodextrins and xyloglucan. The crystal structure of the catalytic domain of NcLPMO9C revealed an extended, highly polar substrate-binding surface well suited to interact with a variety of sugar substrates. The ability of NcLPMO9C to act on soluble substrates was exploited to study enzyme-substrate interactions. EPR studies demonstrated that the Cu(2+) center environment is altered upon substrate binding, whereas isothermal titration calorimetry studies revealed binding affinities in the low micromolar range for polymeric substrates that are due in part to the presence of a carbohydrate-binding module (CBM1). Importantly, the novel structure of NcLPMO9C enabled a comparative study, revealing that the oxidative regioselectivity of LPMO9s (C1, C4, or both) correlates with distinct structural features of the copper coordination sphere. In strictly C1-oxidizing LPMO9s, access to the solvent-facing axial coordination position is restricted by a conserved tyrosine residue, whereas access to this same position seems unrestricted in C4-oxidizing LPMO9s. LPMO9s known to produce a mixture of C1- and C4-oxidized products show an intermediate situation.
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