ReviewApplied microbiology and biotechnology2020
Old yellow enzymes: structures and structure-guided engineering for stereocomplementary bioreduction.
Review in Applied microbiology and biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Redirecting a Native Ene-Reductase Toward Desaturation With Reverse Enantioselectivity.Angewandte Chemie (International ed. in English) · 2026Article
- Light-Driven Enzyme Catalysis: Ultrafast Mechanisms and Biochemical Implications.Biochemistry · 2025Review
- Structural and functional characterization of a new thermophilic-like OYE from Aspergillus flavus.Applied microbiology and biotechnology · 2024Article
- Bilirubin reductase shows host-specific associations in animal large intestines.The ISME journal · 2024Article
- The Structural Biology of Catalase Evolution.Sub-cellular biochemistry · 2024Review
- Expanding the viewpoint: Leveraging sequence information in enzymology.Current opinion in chemical biology · 2023Review
- Article
- RNA-Seq Based Transcriptome Analysis ofJournal of fungi (Basel, Switzerland) · 2022Article
- "A Study in Yellow": Investigations in the Stereoselectivity of Ene-Reductases.Chembiochem : a European journal of chemical biology · 2022Review
- The Old Yellow Enzyme OfrA FostersFrontiers in microbiology · 2022Article
- Engineering of Yeast Old Yellow Enzyme OYE3 Enables Its Capability Discriminating of (Molecules (Basel, Switzerland) · 2021Article
- Visualizing the superfamily of metallo-β-lactamases through sequence similarity network neighborhood connectivity analysis.Heliyon · 2021Article
- Review
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Since the first discovery of old yellow enzyme 1 (OYE1) from Saccharomyces pastorianus in 1932, biocatalytic asymmetric reduction of activated alkenes by OYEs has become a valuable reaction in organic synthesis. To access stereocomplementary C=C-bond bioreduction, the mining of novel OYEs and especially the protein engineering of existing OYEs have been performed, which successfully achieved the stereocomplementary reduction in several cases and further raise the potential of applications. In this review, we analyzed the structures, active sites, and substrate recognition of OYEs, which are the bases for their substrate specificity and stereospecificity. Sequence similarity network of OYEs superfamily was also constructed to investigate the scope of characterized OYEs. The structure-guided engineering to switch the stereoselectivity of OYEs and thus access stereocomplementary bioreduction over the last decade (2009-2020) was then reviewed and discussed, which might give new insights into the mining and engineering of related biocatalysts. KEY POINTS: • The sequence similarity network of OYEs superfamily was constructed and annotated. • The structures and active sites of OYEs from different classes were compared. • "Left/right" binding mode was used to explain the stereopreferences of OYEs. • Structure-guided engineering of OYEs to switch their stereoselectivity was reviewed.
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Registered trials
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