ArticleMicrobial biotechnology2013
Biochemical studies of the multicopper oxidase (small laccase) from Streptomyces coelicolor using bioactive phytochemicals and site-directed mutagenesis.
Article in Microbial biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 54 citations in OpenAlex.
- Coordinated plant and microbial transcriptional responses to oil-sands process-affected water.ISME communications · 2026Article
- Analysis of the electron transfer pathway in small laccase by EPR and UV-vis spectroscopy coupled with redox titration.Magnetic resonance letters · 2024Article
- Structural Insight into the Amino Acid Environment of the Two-Domain Laccase's Trinuclear Copper Cluster.International journal of molecular sciences · 2023Article
- Discovery of lignin-transforming bacteria and enzymes in thermophilic environments using stable isotope probing.The ISME journal · 2022Article
- Article
- Decolorization of Textile Dye by Spore Surface Displayed Small Laccase for the Enhanced Thermal Stability and Robust Repeated Reaction.Biotechnology and bioprocess engineering : BBE · 2022Article
- Efficient Degradation of Aflatoxin BToxins · 2021Article
- A Novel Polyphenol Oxidoreductase OhLac fromFrontiers in microbiology · 2021Article
- Evolved Fusarium oxysporum laccase expressed in Saccharomyces cerevisiae.Scientific reports · 2020Article
- Article
- Biocatalytic Production of Amino Carbohydrates through Oxidoreductase and Transaminase Cascades.ChemSusChem · 2019Article
- Article
- Bacterial laccases: promising biological green tools for industrial applications.Cellular and molecular life sciences : CMLS · 2018Review
- Heterologous expression of a Streptomyces cyaneus laccase for biomass modification applications.AMB Express · 2017Article
- A valuable peroxidase activity from the novel speciesBiotechnology reports (Amsterdam, Netherlands) · 2017Article
- Biofilm and Planktonic Bacterial and Fungal Communities Transforming High-Molecular-Weight Polycyclic Aromatic Hydrocarbons.Applied and environmental microbiology · 2016Article
- Biochemical Characteristics of Three Laccase Isoforms from the Basidiomycete Pleurotus nebrodensis.Molecules (Basel, Switzerland) · 2016Article
- Yeast Hosts for the Production of Recombinant Laccases: A Review.Molecular biotechnology · 2016Review
- Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology.Cellular and molecular life sciences : CMLS · 2015Review
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multicopper oxidases can act on a broad spectrum of phenolic and non-phenolic compounds. These enzymes include laccases, which are widely distributed in plants and fungi, and were more recently identified in bacteria. Here, we present the results of biochemical and mutational studies of small laccase (SLAC), a multicopper oxidase from Streptomyces coelicolor (SCO6712). In addition to typical laccase substrates, SLAC was tested using phenolic compounds that exhibit antioxidant activity. SLAC showed oxidase activity against 12 of 23 substrates tested, including caffeic acid, ferulic acid, resveratrol, quercetin, morin, kaempferol and myricetin. The kinetic parameters of SLAC were determined for 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid), 2,6-dimethoxyphenol, quercetin, morin and myricetin, and maximum reaction rates were observed with myricetin, where kcat and Km values at 60°C were 8.1 (± 0.8) s⁻¹ and 0.9 (± 0.3) mM respectively. SLAC had a broad pH optimum for activity (between pH 4 and 8) and temperature optimum at 60-70°C. It demonstrated remarkable thermostability with a half-life of over 10 h at 80°C and over 7 h at 90°C. Site-directed mutagenesis revealed 17 amino acid residues important for SLAC activity including the 10 His residues involved in copper coordination. Most notably, the Y229A and Y230A mutant proteins showed over 10-fold increase in activity compared with the wild-type SLAC, which was correlated to higher copper incorporation, while kinetic analyses with S929A predicts localization of this residue near the meta-position of aromatic substrates.
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