Engineered Biocatalyst for Enantioselective Hydrazone Reduction

Enantioselective reduction of hydrazones provides a convergent and versatile route to synthesize hydrazine-containing motifs that are commonly found in pharmaceuticals and agrochemicals. However, current methods require the use of precious metals, costly chiral ligands, and/or forcing reaction conditions. Here, we report the development of a biocatalytic approach for enantioselective hydrazone reduction using engineered imine reductases. Following evaluation of an in-house panel of >400 IRED sequences, we identified a single IR361 I127F L179V variant that promotes reduction of Cbz-protected hydrazones. The introduction of additional two mutations via directed evolution afforded HRED1.1 that is 20-fold more active than the parent template and promotes reduction of a variety of protected hydrazones in high yields and selectivities (>99% e.e.), including in preparative scale biotransformations. Structural analysis of HRED1.1 provides insights into the origins of its unique hydrazone reductase activity. This study offers a powerful biocatalytic route to synthesize valuable chiral hydrazine products and further expands the impressive range of transformations accessible with engineered imine reductases.

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Publication Details

Journal
Angewandte Chemie International Edition
Published
2025-04-17
DOI
https://doi.org/10.1002/anie.202424350
Citations
4
Primary Topic
Enzyme Catalysis and Immobilization
Type
article
Field-Weighted Citation Impact
3.22

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article

Engineered Biocatalyst for Enantioselective Hydrazone Reduction

Gideon Grogan, Fei Zhao, Eugene Ho, Phillip D. Clayman et al.
4 citations
Angewandte Chemie International Edition
Enzyme Catalysis and Immobilization
3.22
article

Engineered Biocatalyst for Enantioselective Hydrazone Reduction

Gideon Grogan, Fei Zhao, Eugene Ho, Phillip D. Clayman, Murray J. B. Brown, Vanessa Harawa, Anthony P. Green, Nicholas J. Turner, Amy E. Hutton, J. Domenech
article en
4 citations

Abstract

Enantioselective reduction of hydrazones provides a convergent and versatile route to synthesize hydrazine-containing motifs that are commonly found in pharmaceuticals and agrochemicals. However, current methods require the use of precious metals, costly chiral ligands, and/or forcing reaction conditions. Here, we report the development of a biocatalytic approach for enantioselective hydrazone reduction using engineered imine reductases. Following evaluation of an in-house panel of >400 IRED sequences, we identified a single IR361 I127F L179V variant that promotes reduction of Cbz-protected hydrazones. The introduction of additional two mutations via directed evolution afforded HRED1.1 that is 20-fold more active than the parent template and promotes reduction of a variety of protected hydrazones in high yields and selectivities (>99% e.e.), including in preparative scale biotransformations. Structural analysis of HRED1.1 provides insights into the origins of its unique hydrazone reductase activity. This study offers a powerful biocatalytic route to synthesize valuable chiral hydrazine products and further expands the impressive range of transformations accessible with engineered imine reductases.

Angewandte Chemie International EditionVol. 64(26)
National Nuclear Laboratory (GB), Age UK (GB), University of Manchester (GB), Czech Academy of Sciences, Institute of Biotechnology (CZ), GlaxoSmithKline (India) (IN), Glaxosmithkline (Finland) (FI), GlaxoSmithKline (Ireland) (IE), University of York (GB)
Diamond Light Source, Henry Royce Institute, Engineering and Physical Sciences Research Council
Responsible consumption and production
Openalex Percentile: Top 9%
Enzyme Catalysis and Immobilization
3.22
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