Sequence Similarity Network Guided Discovery of a Dehydrogenase for Asymmetric Carbonyl Dehydrogenation

Abstract Carbonyl dehydrogenation is one of the most valuable transformations in modern synthetic chemistry. As compared to traditional chemical synthesis methods, enzymatic dehydrogenation offers a greener and more selective alternative. However, except for a few rare natural dehydrogenases for desaturation, current enzymatic methods predominantly rely on enzyme promiscuity, which often suffers from lower efficiency and limited reaction controllability. Herein, we employed sequence similarity networks to mine natural dehydrogenases from a vast array of sequences with potential dehydrogenation activity. This approach led to the discovery of an uncharacterized FAD‐dependent enzyme capable of efficiently performing the desymmetrizing desaturation of cyclohexanones, thereby generating diverse cyclohexenones bearing remote γ‐quaternary stereocenters. The current method has enhanced the turnover frequency (TOF) by approximately 178‐fold as compared to the best existing biocatalytic strategies and displayed almost no overoxidation reactions. Through a combination of experimental assays and computational studies, we elucidated that this enzyme enhances its dehydrogenation capability through an unconventional proton relay system, absent in previously reported enzyme promiscuity systems. Additionally, this streamlined enzymatic process demonstrated scalability to gram‐scale synthesis with maintained efficiency and selectivity, offering robust and sustainable alternatives for the synthesis of chiral cyclohexenones with high optical purity.

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Journal
Angewandte Chemie
Published
2025-02-22
DOI
https://doi.org/10.1002/ange.202501425
Primary Topic
Enzyme Catalysis and Immobilization
Type
article
Field-Weighted Citation Impact
0.00

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article

Sequence Similarity Network Guided Discovery of a Dehydrogenase for Asymmetric Carbonyl Dehydrogenation

Zheng Fang, Guixiang Huang, Zhaoxuan Zhu, Hui Wang et al.
1 links
Angewandte Chemie
Enzyme Catalysis and Immobilization
article

Sequence Similarity Network Guided Discovery of a Dehydrogenase for Asymmetric Carbonyl Dehydrogenation

Zheng Fang, Guixiang Huang, Zhaoxuan Zhu, Hui Wang, Wenjing Wang, Zhiguo Wang, Kai Guo, Yuxuan Ye, Jie Chen, Yongzhen Peng, Shaofang Qi, Yujing Hu
article en

Abstract

Abstract Carbonyl dehydrogenation is one of the most valuable transformations in modern synthetic chemistry. As compared to traditional chemical synthesis methods, enzymatic dehydrogenation offers a greener and more selective alternative. However, except for a few rare natural dehydrogenases for desaturation, current enzymatic methods predominantly rely on enzyme promiscuity, which often suffers from lower efficiency and limited reaction controllability. Herein, we employed sequence similarity networks to mine natural dehydrogenases from a vast array of sequences with potential dehydrogenation activity. This approach led to the discovery of an uncharacterized FAD‐dependent enzyme capable of efficiently performing the desymmetrizing desaturation of cyclohexanones, thereby generating diverse cyclohexenones bearing remote γ‐quaternary stereocenters. The current method has enhanced the turnover frequency (TOF) by approximately 178‐fold as compared to the best existing biocatalytic strategies and displayed almost no overoxidation reactions. Through a combination of experimental assays and computational studies, we elucidated that this enzyme enhances its dehydrogenation capability through an unconventional proton relay system, absent in previously reported enzyme promiscuity systems. Additionally, this streamlined enzymatic process demonstrated scalability to gram‐scale synthesis with maintained efficiency and selectivity, offering robust and sustainable alternatives for the synthesis of chiral cyclohexenones with high optical purity.

Angewandte ChemieVol. 137(20)
Nanjing Agricultural University (CN), Nanjing Tech University (CN), Hangzhou Normal University (CN), Westlake University (CN), Département Santé Animale (FR), Institute of Aging (CA), State Key Laboratory of Materials-Oriented Chemical Engineering
National Natural Science Foundation of China, Government of Jiangsu Province, Natural Science Foundation of Jiangsu Province, National Key Research and Development Program of China
Openalex Percentile: Top 97%
Enzyme Catalysis and Immobilization
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