ArticleFrontiers in microbiology2015
Functional characterization and stability improvement of a 'thermophilic-like' ene-reductase from Rhodococcus opacus 1CP.
Article in Frontiers in microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 38 citations in OpenAlex.
- Whole-genomic and transcriptomic analyses elucidateApplied and environmental microbiology · 2026Article
- Structure, Oligomerization, and Thermal Stability of a Recently Discovered Old Yellow Enzyme.Proteins · 2025Article
- Structural and functional characterization of a new thermophilic-like OYE from Aspergillus flavus.Applied microbiology and biotechnology · 2024Article
- Solvent concentration at 50% protein unfolding may reform enzyme stability ranking and process window identification.Nature communications · 2024Article
- The Family Keeps on Growing: Four Novel Fungal OYEs Characterized.International journal of molecular sciences · 2022Article
- A Tailor-Made Deazaflavin-Mediated Recycling System for Artificial Nicotinamide Cofactor Biomimetics.ACS catalysis · 2021Article
- A New Thermophilic Ene-Reductase from the Filamentous Anoxygenic Phototrophic BacteriumMicroorganisms · 2021Article
- Asymmetric Reduction of (R)-Carvone through a Thermostable and Organic-Solvent-Tolerant Ene-Reductase.Chembiochem : a European journal of chemical biology · 2020Article
- Review
- Discovery, Characterisation, Engineering and Applications of Ene Reductases for Industrial Biocatalysis.ACS catalysis · 2019Article
- Editorial:Frontiers in microbiology · 2019Article
- Rhodococcus strains as source for ene-reductase activity.Applied microbiology and biotechnology · 2018Article
- Catalytic Performance of a Class III Old Yellow Enzyme and Its Cysteine Variants.Frontiers in microbiology · 2018Article
- A survey of synthetic nicotinamide cofactors in enzymatic processes.Applied microbiology and biotechnology · 2016Review
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ene-reductases (ERs) are widely applied for the asymmetric synthesis of relevant industrial chemicals. A novel ER OYERo2 was found within a set of 14 putative old yellow enzymes (OYEs) obtained by genome mining of the actinobacterium Rhodococcus opacus 1CP. Multiple sequence alignment suggested that the enzyme belongs to the group of 'thermophilic-like' OYEs. OYERo2 was produced in Escherichia coli and biochemically characterized. The enzyme is strongly NADPH dependent and uses non-covalently bound FMNH2 for the reduction of activated α,β-unsaturated alkenes. In the active form OYERo2 is a dimer. Optimal catalysis occurs at pH 7.3 and 37°C. OYERo2 showed highest specific activities (45-50 U mg(-1)) on maleimides, which are efficiently converted to the corresponding succinimides. The OYERo2-mediated reduction of prochiral alkenes afforded the (R)-products with excellent optical purity (ee > 99%). OYERo2 is not as thermo-resistant as related OYEs. Introduction of a characteristic intermolecular salt bridge by site-specific mutagenesis raised the half-life of enzyme inactivation at 32°C from 28 to 87 min and improved the tolerance toward organic co-solvents. The suitability of OYERo2 for application in industrial biocatalysis is discussed.
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