ArticleACS catalysis2022
Mutations Increasing Cofactor Affinity, Improve Stability and Activity of a Baeyer-Villiger Monooxygenase.
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 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 25 citations in OpenAlex.
- A programmable bifunctional flavoenzyme for direct amine-to-ester conversion.Science advances · 2026Article
- Engineered Oxalate Decarboxylase Boosts Activity and Stability for Biological Applications.ACS omega · 2025Article
- Overcoming a Conceptual Limitation of Industrial ε-Caprolactone Production via Chemoenzymatic Synthesis in Organic Medium.ChemSusChem · 2024Article
- Interfacial Anion-Induced Dispersion of Active Species for Efficient Electrochemical Baeyer-Villiger Oxidation.JACS Au · 2024Article
- On the evolutionary trail of MagRs.Zoological research · 2024Article
- Exploring the role of flavin-dependent monooxygenases in the biosynthesis of aromatic compounds.Biotechnology for biofuels and bioproducts · 2024Review
- A Cold-Active Flavin-Dependent Monooxygenase fromACS catalysis · 2023Article
- The Al-Containing Silicates Modified with Organic Ligands and SnONanomaterials (Basel, Switzerland) · 2023Article
Corrections and comments
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Authors and funding
15 authors at 5 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The typically low thermodynamic and kinetic stability of enzymes is a bottleneck for their application in industrial synthesis. Baeyer-Villiger monooxygenases, which oxidize ketones to lactones using aerial oxygen, among other activities, suffer particularly from these instabilities. Previous efforts in protein engineering have increased thermodynamic stability but at the price of decreased activity. Here, we solved this trade-off by introducing mutations in a cyclohexanone monooxygenase from
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Registered trials
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