ReviewActa biochimica et biophysica Sinica2023
Recent advances in the efficient degradation of lignocellulosic metabolic networks by lytic polysaccharide monooxygenase.
Review in Acta biochimica et biophysica Sinica, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 20 citations in OpenAlex.
- TrLPMO9A drives oxidative cellulose depolymerization in Trichoderma reesei and is enhanced by heterologous cellobiose dehydrogenase expression.Biotechnology for biofuels and bioproducts · 2026Article
- Advances, challenges, and future directions towards a cellulolytic Escherichia coli.Biotechnology for biofuels and bioproducts · 2026Review
- Integrated omics analysis of the cellulose co-degradation network of Chaetomium thermophilum.Biotechnology for biofuels and bioproducts · 2026Article
- Genomic and Transcriptomic Insights into Carbon-Source and Temporal Induction of a Diverse Set of Lignocellulolytic Enzymes inJournal of fungi (Basel, Switzerland) · 2025Article
- Discovery of a novel marine Bacteroidetes with a rich repertoire of carbohydrate-active enzymes.Computational and structural biotechnology journal · 2024Article
- The impact of the carbohydrate-binding module on how a lytic polysaccharide monooxygenase modifies cellulose fibers.Biotechnology for biofuels and bioproducts · 2024Article
- Heterologous Expression and Biochemical Characterization of a Novel Lytic Polysaccharide Monooxygenase fromMicroorganisms · 2024Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Along with long-term evolution, the plant cell wall generates lignocellulose and other anti-degradation barriers to confront hydrolysis by fungi. Lytic polysaccharide monooxygenase (LPMO) is a newly defined oxidase in lignocellulosic degradation systems that significantly fuels hydrolysis. LPMO accepts electrons from wide sources, such as cellobiose dehydrogenase (CDH), glucose-methanol-choline (GMC) oxidoreductases, and small phenols. In addition, the extracellular cometabolic network formed by cosubstrates improves the degradation efficiency, forming a stable and efficient lignocellulose degradation system. In recent years, using structural proteomics to explore the internal structure and the complex redox system of LPMOs has become a research hotspot. In this review, the diversity of LPMOs, catalytic domains, carbohydrate binding modules, direct electron transfer with CDH, cosubstrates, and degradation networks of LPMOs are explored, which can provide a systematic reference for the application of lignocellulosic degradation systems in industrial approaches.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.