One-Pot Chemoenzymatic Synthesis of Arsinothricin and the Mechanistic Insights into the Noncanonical Radical SAM Enzyme ArsL

Arsinothricin (AST) is a broad-spectrum arsenic-containing antibiotic with promising pharmaceutical properties. In this study, we report the one-pot chemoenzymatic synthesis of AST starting from methylarsenate, a commonly used agricultural herbicide. Although a single point mutation in the C-terminal region of ArsL completely abolished its activity toward the natural substrate inorganic arsenite, this mutation unexpectedly enhanced its activity toward methylarsenate by over 50-fold, enabling subgram scale production of AST in a cell-free system. These findings offer valuable mechanistic insights into ArsL and highlight the significant potential of manipulating the radical SAM superfamily enzymes in synthetic applications.

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Publication Details

Journal
ACS Catalysis
Published
2024-12-19
DOI
https://doi.org/10.1021/acscatal.4c04938
Citations
4
Primary Topic
Metalloenzymes and iron-sulfur proteins
Type
article
Field-Weighted Citation Impact
0.41

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article

One-Pot Chemoenzymatic Synthesis of Arsinothricin and the Mechanistic Insights into the Noncanonical Radical SAM Enzyme ArsL

Fen‐Er Chen, Qi Zhang, Wei Ding, Li He
4 citations
ACS Catalysis
Metalloenzymes and iron-sulfur proteins
0.41
article

One-Pot Chemoenzymatic Synthesis of Arsinothricin and the Mechanistic Insights into the Noncanonical Radical SAM Enzyme ArsL

Fen‐Er Chen, Qi Zhang, Wei Ding, Li He
article en
4 citations

Abstract

Arsinothricin (AST) is a broad-spectrum arsenic-containing antibiotic with promising pharmaceutical properties. In this study, we report the one-pot chemoenzymatic synthesis of AST starting from methylarsenate, a commonly used agricultural herbicide. Although a single point mutation in the C-terminal region of ArsL completely abolished its activity toward the natural substrate inorganic arsenite, this mutation unexpectedly enhanced its activity toward methylarsenate by over 50-fold, enabling subgram scale production of AST in a cell-free system. These findings offer valuable mechanistic insights into ArsL and highlight the significant potential of manipulating the radical SAM superfamily enzymes in synthetic applications.

ACS CatalysisVol. 15(1)
Shanghai Jiao Tong University (CN), Fudan University (CN), Ecologie microbienne (FR), Chemical Synthesis Lab (SG), Jiangxi Normal University (CN)
National Natural Science Foundation of China, Shanghai Municipal Education Commission, West Light Foundation of the Chinese Academy of Sciences
Openalex Percentile: Top 46%
Metalloenzymes and iron-sulfur proteins
0.41
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One-Pot Chemoenzymatic Synthesis of Arsinothricin and the Mechanistic Insights into the Noncanonical Radical SAM Enzyme ArsL — Fen‐Er Chen, Qi Zhang, et al. · ACS Catalysis (2024) | TGRS Research Map | TGRS