ArticlePloS one2013
Laccase versus laccase-like multi-copper oxidase: a comparative study of similar enzymes with diverse substrate spectra.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed, 223 citations in OpenAlex.
- Genome-Wide Identification, Expression Profiling, and microRNA397-Mediated Regulation of Laccase Genes inPlants (Basel, Switzerland) · 2026Article
- Understanding Lignin Oxidation by a Two-Domain Multicopper Oxidase fromBiochemistry · 2026Article
- Genome-wide characterization of the LAC gene family in five fern species reveals evolutionary diversification and putative roles in lignin biosynthesis in Alsophila spinulosa.BMC plant biology · 2026Article
- Machine Learning Prediction of Laccase-Catalyzed Oxidation of Aromatic Compounds Using Curated Enzyme-Specific Datasets.Journal of computational chemistry · 2026Article
- Adaptive evolution of Agaricomycetes laccases follows wood lignin diversification in plants.Applied and environmental microbiology · 2026Article
- Optimized production of laccase from Pseudomonas stutzeri and its biodegradation of lignin in biomass.Folia microbiologica · 2025Article
- Article
- Enhanced discovery of bacterial laccase-like multicopper oxidase through computer simulation and metagenomic analysis of industrial wastewater.FEBS open bio · 2025Article
- Cloning, Characterization, and Computer-Aided Evolution of a Thermostable Laccase of the DUF152 Family From Klebsiella michiganensis.Proteins · 2025Article
- Lignin-Degrading Enzymes and the Potential ofMicroorganisms · 2025Review
- Characterization and evaluation of the immobilized laccase enzyme potential in dye degradation via one factor and response surface methodology approaches.Scientific reports · 2025Article
- Comprehensive Genomic and Proteomic Analysis Identifies Effectors ofJournal of fungi (Basel, Switzerland) · 2024Article
- In Silico Identification of the Laccase-Encoding Gene in the Transcriptome of the Amazon River PrawnGenes · 2024Article
- Review
- Pollutant profile complexity governs wastewater removal of recalcitrant pharmaceuticals.The ISME journal · 2024Article
- Fungal Laccases: Fundamentals, Engineering and Classification Update.Biomolecules · 2023Review
- Phenoloxidases: catechol oxidase - the temporary employer and laccase - the rising star of vascular plants.Horticulture research · 2023Article
- Molecular Docking of Lac_CB10: Highlighting the Great Potential for Bioremediation of Recalcitrant Chemical Compounds by One Predicted Bacteroidetes CopA-Laccase.International journal of molecular sciences · 2023Article
- A Genome-Wide Identification and Expression Pattern ofPlants (Basel, Switzerland) · 2023Article
- Comprehensive analysis of the laccase gene family in tea plant highlights its roles in development and stress responses.BMC plant biology · 2023Article
24 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Laccases (EC 1.10.3.2) are multi-copper oxidases that catalyse the one-electron oxidation of a broad range of compounds including substituted phenols, arylamines and aromatic thiols to the corresponding radicals. Owing to their broad substrate range, copper-containing laccases are versatile biocatalysts, capable of oxidizing numerous natural and non-natural industry-relevant compounds, with water as the sole by-product. In the present study, 10 of the 11 multi-copper oxidases, hitherto considered to be laccases, from fungi, plant and bacterial origin were compared. A substrate screen of 91 natural and non-natural compounds was recorded and revealed a fairly broad but distinctive substrate spectrum amongst the enzymes. Even though the enzymes share conserved active site residues we found that the substrate ranges of the individual enzymes varied considerably. The EC classification is based on the type of chemical reaction performed and the actual name of the enzyme often refers to the physiological substrate. However, for the enzymes studied in this work such classification is not feasible, even more so as their prime substrates or natural functions are mainly unknown. The classification of multi-copper oxidases assigned as laccases remains a challenge. For the sake of simplicity we propose to introduce the term "laccase-like multi-copper oxidase" (LMCO) in addition to the term laccase that we use exclusively for the enzyme originally identified from the sap of the lacquer tree Rhus vernicifera.
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