ArticlePloS one2020
"Yellow" laccase from Sclerotinia sclerotiorum is a blue laccase that enhances its substrate affinity by forming a reversible tyrosyl-product adduct.
Article in PloS one, 2020. 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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12 citing papers in PubMed, 31 citations in OpenAlex.
- Blue and Yellow Laccases fromJournal of fungi (Basel, Switzerland) · 2024Article
- Anthracene detoxification by Laccases from indigenous fungal strains Trichoderma lixii FLU1 and Talaromyces pinophilus FLU12.Biodegradation · 2024Article
- Purification, characterization and three-dimensional structure prediction of multicopper oxidase Laccases from Trichoderma lixii FLU1 and Talaromyces pinophilus FLU12.Scientific reports · 2024Article
- Lignin degradation by a novel thermophilic and alkaline yellow laccase fromMicrobiology spectrum · 2024Article
- Exploring laccase: a sustainable enzymatic solution for the paper recycling domain.Archives of microbiology · 2024Review
- Wheat bran as an efficient agro-process waste for enhanced yellow laccase production by3 Biotech · 2024Article
- Formation of a Purple Product upon the Reaction of ABTS Radicals with Proteins.International journal of molecular sciences · 2023Article
- Potential of the enzyme laccase for the synthesis and derivatization of antimicrobial compounds.World journal of microbiology & biotechnology · 2023Review
- 2,4-Dichlorophenol biotransformation using immobilized marine halophilic Bacillus subtilis culture and laccase enzyme: application in wastewater treatment.Journal, genetic engineering & biotechnology · 2022Article
- Laccases and Tyrosinases in Organic Synthesis.International journal of molecular sciences · 2022Review
- Laccases as green and versatile biocatalysts: from lab to enzyme market-an overview.Bioresources and bioprocessing · 2021Review
- Characterization of a Yellow Laccase fromJournal of fungi (Basel, Switzerland) · 2021Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Yellow laccases lack the typical blue type 1 Cu absorption band around 600 nm; however, multi-copper oxidases with laccase properties have been reported. We provide the first evidence that the yellow laccase isolated from Sclerotinia sclerotiorum is obtained from a blue form by covalent, but nevertheless reversible modification with a phenolic product. After separating the phenolics from the extracellular medium, a typical blue laccase is obtained. With ABTS as model substrate for this blue enzyme, a non-natural purple adduct is formed with a spectrum nearly identical to that of the 1:1 adduct of an ABTS radical and Tyr. This modification significantly increases the stability and substrate affinity of the enzyme, not by acting primarily as bound mediator, but by structural changes that also alters the type 1 Cu site. The HPLC-MS analyses of the ABTS adduct trypsin digests revealed a distinct tyrosine within a unique loop as site involved in the modification of the blue laccase form. Thus, S. sclerotiorum yellow laccase seems to be an intrinsically blue multi-copper oxidase that boosts its activity and stability with a radical-forming aromatic substrate. This particular case could, at least in part, explain the enigma of the yellow laccases.
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