ArticleApplied and environmental microbiology2003
A novel extracellular multicopper oxidase from Phanerochaete chrysosporium with ferroxidase activity.
Article in Applied and environmental microbiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 116 citations in OpenAlex.
- Altering the Properties of Laccases fromBiomolecules · 2025Article
- The Rhizophagus irregularis permease RiFTR1 functions without a ferroxidase partner for reductive iron transport.Scientific reports · 2025Article
- Fungal Laccases: Fundamentals, Engineering and Classification Update.Biomolecules · 2023Review
- Genome-wide study of Cerrena unicolor 87613 laccase gene family and their mode prediction in association with substrate oxidation.BMC genomics · 2023Article
- Lessons on fruiting body morphogenesis from genomes and transcriptomes ofStudies in mycology · 2023Article
- Multicopper oxidases with laccase-ferroxidase activity: Classification and study of ferroxidase activity determinants in a member fromComputational and structural biotechnology journal · 2023Article
- Genes Identification, Molecular Docking and Dynamics Simulation Analysis of Laccases fromInternational journal of molecular sciences · 2020Article
- Multicopper Oxidases inJournal of fungi (Basel, Switzerland) · 2020Review
- Systematic Analysis of the Pleurotus ostreatus Laccase Gene (PoLac) Family and Functional Characterization of PoLac2 Involved in the Degradation of Cotton-Straw Lignin.Molecules (Basel, Switzerland) · 2018Article
- Whole-GenomeGenome announcements · 2017Article
- Regulation of Gene Expression during the Onset of Ligninolytic Oxidation by Phanerochaete chrysosporium on Spruce Wood.Applied and environmental microbiology · 2015Article
- Identification and characterization of laccase-type multicopper oxidases involved in dye-decolorization by the fungus Leptosphaerulina sp.BMC biotechnology · 2015Article
- Characterization of pH dependent Mn(II) oxidation strategies and formation of a bixbyite-like phase by Mesorhizobium australicum T-G1.Frontiers in microbiology · 2015Article
- Analysis of the Phlebiopsis gigantea genome, transcriptome and secretome provides insight into its pioneer colonization strategies of wood.PLoS genetics · 2014Article
- Cloning, characterization and expression of a novel laccase gene Pclac2 from Phytophthora capsici.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2014Article
- LacSubPred: predicting subtypes of Laccases, an important lignin metabolism-related enzyme class, using in silico approaches.BMC bioinformatics · 2014Article
- Multiple multi-copper oxidase gene families in basidiomycetes - what for?Current genomics · 2011Article
- Exploring laccase-like multicopper oxidase genes from the ascomycete Trichoderma reesei: a functional, phylogenetic and evolutionary study.BMC biochemistry · 2010Article
- Directed evolution of copper nitrite reductase to a chromogenic reductant.Protein engineering, design & selection : PEDS · 2010Article
- Laccases: a never-ending story.Cellular and molecular life sciences : CMLS · 2010Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lignin degradation by the white rot basidiomycete Phanerochaete chrysosporium involves various extracellular oxidative enzymes, including lignin peroxidase, manganese peroxidase, and a peroxide-generating enzyme, glyoxal oxidase. Recent studies have suggested that laccases also may be produced by this fungus, but these conclusions have been controversial. We identified four sequences related to laccases and ferroxidases (Fet3) in a search of the publicly available P. chrysosporium database. One gene, designated mco1, has a typical eukaryotic secretion signal and is transcribed in defined media and in colonized wood. Structural analysis and multiple alignments identified residues common to laccase and Fet3 sequences. A recombinant MCO1 (rMCO1) protein expressed in Aspergillus nidulans had a molecular mass of 78 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the copper I-type center was confirmed by the UV-visible spectrum. rMCO1 oxidized various compounds, including 2,2'-azino(bis-3-ethylbenzthiazoline-6-sulfonate) (ABTS) and aromatic amines, although phenolic compounds were poor substrates. The best substrate was Fe2+, with a Km close to 2 micro M. Collectively, these results suggest that the P. chrysosporium genome does not encode a typical laccase but rather encodes a unique extracellular multicopper oxidase with strong ferroxidase activity.
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