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Biocatalytic reductions and chemical versatility of the old yellow enzyme family of flavoprotein oxidoreductases
The old yellow enzyme (OYE) family is a large group of flavin‐dependent redox biocatalysts
with major applications in the industrial reduction of activated alkenes. These enzymes have …
with major applications in the industrial reduction of activated alkenes. These enzymes have …
Enantioenriched compounds via enzyme-catalyzed redox reactions
Redox reactions are essential to any currently known form of life and are at the core of a
majority of metabolic processes, such as cellular respiration or photosynthesis. As about …
majority of metabolic processes, such as cellular respiration or photosynthesis. As about …
Tailored photoenzymatic systems for selective reduction of aliphatic and aromatic nitro compounds fueled by light
AP Luján, MF Bhat, S Tsaturyan, R van Merkerk… - Nature …, 2023 - nature.com
The selective enzymatic reduction of nitroaliphatic and nitroaromatic compounds to aliphatic
amines and amino-, azoxy-and azo-aromatics, respectively, remains a persisting challenge …
amines and amino-, azoxy-and azo-aromatics, respectively, remains a persisting challenge …
Old yellow enzyme-catalysed asymmetric hydrogenation: linking family roots with improved catalysis
A Scholtissek, D Tischler, AH Westphal… - Catalysts, 2017 - mdpi.com
Asymmetric hydrogenation of activated alkenes catalysed by ene-reductases from the old
yellow enzyme family (OYEs) leading to chiral products is of potential interest for industrial …
yellow enzyme family (OYEs) leading to chiral products is of potential interest for industrial …
Directed evolution of an enantioselective enoate‐reductase: testing the utility of iterative saturation mutagenesis
DJ Bougioukou, S Kille, A Taglieber… - Advanced synthesis & …, 2009 - Wiley Online Library
Directed evolution utilizing iterative saturation mutagenesis (ISM) has been applied to the
old yellow enzyme homologue YqjM in the quest to broaden its substrate scope, while …
old yellow enzyme homologue YqjM in the quest to broaden its substrate scope, while …
Asymmetric catalysis with an inert chiral-at-metal iridium complex
The development of a chiral-at-metal iridium (III) complex for the highly efficient catalytic
asymmetric transfer hydrogenation of β, β′-disubstituted nitroalkenes is reported. Catalysis …
asymmetric transfer hydrogenation of β, β′-disubstituted nitroalkenes is reported. Catalysis …
Catalytic asymmetric conjugate reduction
G Lonardi, R Parolin, G Licini… - Angewandte Chemie …, 2023 - Wiley Online Library
Enantioselective reduction reactions are privileged transformations for the construction of
trisubstituted stereogenic centers. While these include established synthetic strategies, such …
trisubstituted stereogenic centers. While these include established synthetic strategies, such …
Biocatalysis with thermostable enzymes: structure and properties of a thermophilic 'ene'‐reductase related to old yellow enzyme
We report the crystal structure of a thermophilic “ene” reductase (TOYE) isolated from
Thermoanaerobacter pseudethanolicus E39. The crystal structure reveals a tetrameric …
Thermoanaerobacter pseudethanolicus E39. The crystal structure reveals a tetrameric …
Asymmetric reduction of activated alkenes by pentaerythritol tetranitrate reductase: specificity and control of stereochemical outcome by reaction optimisation
We show that pentaerythritol tetranitrate reductase (PETNR), a member of the 'ene'reductase
old yellow enzyme family, catalyses the asymmetric reduction of a variety of industrially …
old yellow enzyme family, catalyses the asymmetric reduction of a variety of industrially …
Asymmetric reductive carbocyclization using engineered ene reductases
K Heckenbichler, A Schweiger… - Angewandte Chemie …, 2018 - Wiley Online Library
Ene reductases from the Old Yellow Enzyme (OYE) family reduce the C= C double bond in
α, β‐unsaturated compounds bearing an electron‐withdrawing group, for example, a …
α, β‐unsaturated compounds bearing an electron‐withdrawing group, for example, a …