Engineering an <scp>l</scp> -Threonine Aldolase from <i>Staphylococcus epidermidis</i> for Enhanced Diastereoselectivity in the Synthesis of a Chloramphenicol Intermediate

. Furthermore, Mut4 exhibits markedly improved diastereoselectivity toward para- and meta-substituted benzaldehyde derivatives. Molecular dynamics (MD) simulations further elucidated the molecular basis underlying the enhanced diastereoselectivity of Mut4. This study provides a potential biocatalyst for the sustainable and efficient synthesis of a chloramphenicol intermediate.

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Publication Details

Journal
Journal of Agricultural and Food Chemistry
Published
2026-04-10
DOI
https://doi.org/10.1021/acs.jafc.6c01578
Primary Topic
Enzyme Structure and Function
Type
article
Field-Weighted Citation Impact
0.00

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article

Engineering an l -Threonine Aldolase from Staphylococcus epidermidis for Enhanced Diastereoselectivity in the Synthesis of a Chloramphenicol Intermediate

Xinglu Zhu, Di Wei, Yifang Meng, Shuya Sun et al.
Journal of Agricultural and Food Chemistry
Enzyme Structure and Function
article

Engineering an l -Threonine Aldolase from Staphylococcus epidermidis for Enhanced Diastereoselectivity in the Synthesis of a Chloramphenicol Intermediate

Xinglu Zhu, Di Wei, Yifang Meng, Shuya Sun, Feiyang Deng
article en

Abstract

. Furthermore, Mut4 exhibits markedly improved diastereoselectivity toward para- and meta-substituted benzaldehyde derivatives. Molecular dynamics (MD) simulations further elucidated the molecular basis underlying the enhanced diastereoselectivity of Mut4. This study provides a potential biocatalyst for the sustainable and efficient synthesis of a chloramphenicol intermediate.

Journal of Agricultural and Food ChemistryVol. 74(15)
East China University of Science and Technology (CN)
Science and Technology Commission of Shanghai Municipality
Responsible consumption and production
Openalex Percentile: Top 22%
Enzyme Structure and Function
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