ArticleACS catalysis2022
Designed High-Redox Potential Laccases Exhibit High Functional Diversity.
Article in ACS catalysis, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Review
- Hydrophobic tuning with non-canonical amino acids in a copper metalloenzyme.Nature chemistry · 2026Article
- Strategies for recombinant laccase expression and their roles in environmental remediation.World journal of microbiology & biotechnology · 2026Review
- Bacterial laccases for green remediation of contaminants of emerging concern: from molecular cloning to metagenomic and computational insights.Biodegradation · 2026Review
- SubTuner leverages physics-based modeling to complement AI in enzyme engineering toward non-native substrates.Chem catalysis · 2025Article
- Enzyme Enhancement Through Computational Stability Design Targeting NMR-Determined Catalytic Hotspots.Journal of the American Chemical Society · 2025Article
- Stable and Promiscuous Galactose Oxidases Engineered by Directed Evolution, Atomistic Design, and Ancestral Sequence Reconstruction.ACS synthetic biology · 2025Article
- Enhanced extracellular production of Coprinopsis cinerea laccase Lcc9 in Aspergillus niger by gene expression cassette and bioprocess optimization.BMC biotechnology · 2024Article
- Enhancing catalytic efficiency of Bacillus subtilis laccase BsCotA through active site pocket design.Applied microbiology and biotechnology · 2024Article
- Addressing epistasis in the design of protein function.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Analysis of the electron transfer pathway in small laccase by EPR and UV-vis spectroscopy coupled with redox titration.Magnetic resonance letters · 2024Article
- Enhanced extracellular production of laccase in Coprinopsis cinerea by silencing chitinase gene.Applied microbiology and biotechnology · 2024Article
- Opportunities and Challenges for Machine Learning-Assisted Enzyme Engineering.ACS central science · 2024Review
- Increasing Reduction Potentials of Type 1 Copper Center and Catalytic Efficiency of Small Laccase from Streptomyces coelicolor through Secondary Coordination Sphere Mutations.Angewandte Chemie (International ed. in English) · 2023Article
- Laccase Engineering: Redox Potential Is Not the Only Activity-Determining Feature in the Metalloproteins.Molecules (Basel, Switzerland) · 2023Review
- Structural Insight into the Amino Acid Environment of the Two-Domain Laccase's Trinuclear Copper Cluster.International journal of molecular sciences · 2023Article
- An Inferred Ancestral CotA Laccase with Improved Expression and Kinetic Efficiency.International journal of molecular sciences · 2023Article
- Designed active-site library reveals thousands of functional GFP variants.Nature communications · 2023Article
- De Novo Computational Design of a Lipase with Hydrolysis Activity towards Middle-Chained Fatty Acid Esters.International journal of molecular sciences · 2023Article
- Repertoire of Computationally Designed Peroxygenases for Enantiodivergent C-H Oxyfunctionalization Reactions.Journal of the American Chemical Society · 2023Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
White-rot fungi secrete an impressive repertoire of high-redox potential laccases (HRPLs) and peroxidases for efficient oxidation and utilization of lignin. Laccases are attractive enzymes for the chemical industry due to their broad substrate range and low environmental impact. Since expression of functional recombinant HRPLs is challenging, however, iterative-directed evolution protocols have been applied to improve their expression, activity, and stability. We implement a rational, stabilize-and-diversify strategy to two HRPLs that we could not functionally express. First, we use the PROSS stability-design algorithm to allow functional expression in yeast. Second, we use the stabilized enzymes as starting points for FuncLib active-site design to improve their activity and substrate diversity. Four of the FuncLib-designed HRPLs and their PROSS progenitor exhibit substantial diversity in reactivity profiles against high-redox potential substrates, including lignin monomers. Combinations of 3-4 subtle mutations that change the polarity, solvation, and sterics of the substrate-oxidation site result in orders of magnitude changes in reactivity profiles. These stable and versatile HRPLs are a step toward generating an effective lignin-degrading consortium of enzymes that can be secreted from yeast. The stabilize-and-diversify strategy can be applied to other challenging enzyme families to study and expand the utility of natural enzymes.
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Registered trials
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