ArticleFrontiers in microbiology2015
Diversity of laccase-coding genes in Fusarium oxysporum genomes.
Article in Frontiers in microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 26 citations in OpenAlex.
- Decoding the distribution, structure-function-redox potential relationship and recent advances in fungal laccases: a systematic approach.Bioprocess and biosystems engineering · 2026Review
- Characterization and application potential of a robust recombinant laccase rTpLcc3 from Trametes polyzona for textile dye decolorization.Scientific reports · 2026Article
- Genome-enabled discovery of candidate virulence loci in Striga hermonthica, a devastating parasite of African cereal crops.The New phytologist · 2022Article
- Comparative transcriptome analysis reveals the resistance regulation mechanism and fungicidal activity of the fungicide phenamacril in Fusarium oxysporum.Scientific reports · 2022Article
- Bioaugmentation of Native Fungi, an Efficient Strategy for the Bioremediation of an Aged Industrially Polluted Soil With Heavy Hydrocarbons.Frontiers in microbiology · 2021Article
- Predicting Virulence ofToxins · 2020Article
- Production of polyextremotolerant laccase byBiotechnology reports (Amsterdam, Netherlands) · 2019Article
- Improvement of efficiency of brown coal biosolubilization by novel recombinant Fusarium oxysporum laccase.AMB Express · 2018Article
- Phylogenomic analyses reveal the diversity of laccase-coding genes in Fonsecaea genomes.PloS one · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multiple studies confirm laccase role in fungal pathogenicity and lignocellulose degradation. In spite of broad genomic research, laccases from plant wilt pathogen Fusarium oxysporum are still not characterized. The study aimed to identify F. oxysporum genes that may encode laccases sensu stricto and to characterize the proteins in silico in order to facilitate further research on their impact on the mentioned processes. Twelve sequenced F. oxysporum genomes available on Broad Institute of Harvard and MIT (2015) website were analyzed and three genes that may encode laccases sensu stricto were found. Their amino acid sequences possess all features essential for their catalytic activity, moreover, the homology models proved the characteristic 3D laccase structures. The study shades light on F. oxysporum as a new source of multicopper oxidases, enzymes with possible high redox potential and broad perspective in biotechnological applications.
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