ArticlePloS one2018
Functional characterization of a lytic polysaccharide monooxygenase from the thermophilic fungus Myceliophthora thermophila.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 50 citations in OpenAlex.
- Transcription factor MtCLR-2 regulates cellulase production via direct modulation of Mtegl2 and Mtbgl1 expression in Myceliophthora thermophila.Microbial cell factories · 2026Article
- Lytic Polysaccharide Monooxygenase fromInternational journal of molecular sciences · 2021Article
- Oxidative Power: Tools for Assessing LPMO Activity on Cellulose.Biomolecules · 2021Review
- Harnessing microbial wealth for lignocellulose biomass valorization through secretomics: a review.Biotechnology for biofuels · 2021Review
- LPMOInternational journal of molecular sciences · 2020Article
- Quantitative comparison of the biomass-degrading enzyme repertoires of five filamentous fungi.Scientific reports · 2020Article
- Article
- Configuration of active site segments in lytic polysaccharide monooxygenases steers oxidative xyloglucan degradation.Biotechnology for biofuels · 2020Article
- Insights into an unusual Auxiliary Activity 9 family member lacking the histidine brace motif of lytic polysaccharide monooxygenases.The Journal of biological chemistry · 2019Article
- Multidisciplinary involvement and potential of thermophiles.Folia microbiologica · 2019Review
- An actinobacteria lytic polysaccharide monooxygenase acts on both cellulose and xylan to boost biomass saccharification.Biotechnology for biofuels · 2019Article
- On the functional characterization of lytic polysaccharide monooxygenases (LPMOs).Biotechnology for biofuels · 2019Review
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thermophilic fungi are a promising source of thermostable enzymes able to hydrolytically or oxidatively degrade plant cell wall components. Among these enzymes are lytic polysaccharide monooxygenases (LPMOs), enzymes capable of enhancing biomass hydrolysis through an oxidative mechanism. Myceliophthora thermophila (synonym Sporotrichum thermophile), an Ascomycete fungus, expresses and secretes over a dozen different LPMOs. In this study, we report the overexpression and biochemical study of a previously uncharacterized LPMO (MtLPMO9J) from M. thermophila M77 in Aspergillus nidulans. MtLPMO9J is a single-domain LPMO and has 63% sequence similarity with the catalytic domain of NcLPMO9C from Neurospora crassa. Biochemical characterization of MtLPMO9J revealed that it performs C4-oxidation and is active against cellulose, soluble cello-oligosaccharides and xyloglucan. Moreover, biophysical studies showed that MtLPMO9J is structurally stable at pH above 5 and at temperatures up to 50°C. Importantly, LC-MS analysis of the peptides after tryptic digestion of the recombinantly produced protein revealed not only the correct processing of the signal peptide and methylation of the N-terminal histidine, but also partial autoxidation of the catalytic center. This shows that redox conditions need to be controlled, not only during LPMO reactions but also during protein production, to protect LPMOs from oxidative damage.
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