Ene-Reductase-Catalyzed Oxidation Reactions
Jacob M.A. van Hengst (TU Delft - BT/Biocatalysis)
Allison Wolder (TU Delft - BT/Biocatalysis)
M.K. Sánchez (TU Delft - BT/Biocatalysis)
M.M.E. Huijbers (TU Delft - BT/Biocatalysis)
Diederik J. Opperman (University of the Free State)
Pierre Gilles (Protéus – Seqens)
Juliette Martin (Protéus – Seqens)
T. Hilberath (TU Delft - BT/Biocatalysis)
F. Hollmann (TU Delft - BT/Biocatalysis)
CE Paul (TU Delft - BT/Biocatalysis)
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Abstract
Ene-reductases from the old yellow enzyme (OYE) family have been traditionally employed in the reduction of conjugated C═C double bonds. This study explores the underutilized oxidative potential of OYEs, demonstrating their capability to catalyze the enantioselective desaturation of carbonyl compounds. Utilizing a deprotonated tyrosine residue as a catalytic base, we developed a method to enable OYE-catalyzed desaturation at ambient temperature and alkaline pH without the need for high-temperature conditions. Through screening of various OYE enzymes, we identified several candidates from different genera with enhanced desaturase activity across different substrates. This work broadens the scope of biocatalytic applications for OYEs, introducing a novel approach to the synthesis of chiral α,β-unsaturated carbonyl compounds.
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