Ene-Reductase-Catalyzed Oxidation Reactions

Jacob M.A. van Hengst; Allison E. Wolder; Marisa Sánchez; Mieke M.E. Huijbers; Diederik J. Opperman; Pierre Gilles; Juliette Martin; Thomas Hilberath; Frank Hollmann; Caroline E. Paul

doi:10.1002/cctc.202401447

Ene-Reductase-Catalyzed Oxidation Reactions

Jacob M.A. van Hengst, Allison E. Wolder, Marisa Sánchez, Mieke M.E. Huijbers, Diederik J. Opperman, Pierre Gilles, Juliette Martin, Thomas Hilberath, Frank Hollmann^*, Caroline E. Paul^*

^*Corresponding author for this work

BT/Biocatalysis

Research output: Contribution to journal › Article › Scientific › peer-review

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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.

Original language	English
Number of pages	5
Journal	ChemCatChem
DOIs	https://doi.org/10.1002/cctc.202401447
Publication status	Published - 2024

Keywords

Biocatalysis
Desaturation
Kinetic resolution
Old yellow enzyme
Oxidation

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10.1002/cctc.202401447

ChemCatChem - 2024 - Hengst - Ene‐Reductase‐Catalyzed Oxidation ReactionsFinal published version, 1.25 MBLicence: CC BY

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title = "Ene-Reductase-Catalyzed Oxidation Reactions",

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.",

keywords = "Biocatalysis, Desaturation, Kinetic resolution, Old yellow enzyme, Oxidation",

author = "{van Hengst}, {Jacob M.A.} and Wolder, {Allison E.} and Marisa S{\'a}nchez and Huijbers, {Mieke M.E.} and Opperman, {Diederik J.} and Pierre Gilles and Juliette Martin and Thomas Hilberath and Frank Hollmann and Paul, {Caroline E.}",

year = "2024",

doi = "10.1002/cctc.202401447",

language = "English",

journal = "ChemCatChem",

issn = "1867-3880",

publisher = "Wiley",

}

TY - JOUR

T1 - Ene-Reductase-Catalyzed Oxidation Reactions

AU - van Hengst, Jacob M.A.

AU - Wolder, Allison E.

AU - Sánchez, Marisa

AU - Huijbers, Mieke M.E.

AU - Opperman, Diederik J.

AU - Gilles, Pierre

AU - Martin, Juliette

AU - Hilberath, Thomas

AU - Hollmann, Frank

AU - Paul, Caroline E.

PY - 2024

Y1 - 2024

N2 - 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.

AB - 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.

KW - Biocatalysis

KW - Desaturation

KW - Kinetic resolution

KW - Old yellow enzyme

KW - Oxidation

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U2 - 10.1002/cctc.202401447

DO - 10.1002/cctc.202401447

M3 - Article

AN - SCOPUS:85205101555

SN - 1867-3880

JO - ChemCatChem

JF - ChemCatChem

ER -

Ene-Reductase-Catalyzed Oxidation Reactions

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Keywords

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