Sulfation in the Biosynthesis of the Heptadecaglycoside Antibiotic Saccharomicin A

Sulfation is a ubiquitous modification in glycobiology, yet its enzymology and biological significance in glycosylated natural products remain poorly understood. Saccharomicin A, a potent oligosaccharide antibiotic, carries 17 sugars including a unique sulfated fucose. Here, we report the identification of Sam10 as an unprecedented fucose-specific sulfotransferase through genetic studies, in vitro reconstitution, and structural analysis, establishing its role in saccharomicin sulfation. Comparative bioassays revealed that sulfation contributes to antibacterial potency, including activity against diverse multidrug-resistant pathogens. We also characterized Sam35 as an efficient adenylyl-sulfate kinase that boosts cellular 3′-phosphoadenosine-5′-phosphate sulfate (PAPS) supply. Our findings define the biochemical and structural basis of saccharomicin sulfation and provide enzymatic tools for engineering novel sulfated oligosaccharide antibiotics.

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Publication Details

Journal
JACS Au
Published
2026-05-23
DOI
https://doi.org/10.1021/jacsau.6c00414
Primary Topic
Carbohydrate Chemistry and Synthesis
Type
article
Field-Weighted Citation Impact
0.00

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article

Sulfation in the Biosynthesis of the Heptadecaglycoside Antibiotic Saccharomicin A

崔丽, W Ding, Sijia Guo, Zixin Deng et al.
JACS Au
Carbohydrate Chemistry and Synthesis
article

Sulfation in the Biosynthesis of the Heptadecaglycoside Antibiotic Saccharomicin A

崔丽, W Ding, Sijia Guo, Zixin Deng, Qi Zhang, Wei Zhang, Peng Sun, Yanyi Piao, Yang Cao
article en

Abstract

Sulfation is a ubiquitous modification in glycobiology, yet its enzymology and biological significance in glycosylated natural products remain poorly understood. Saccharomicin A, a potent oligosaccharide antibiotic, carries 17 sugars including a unique sulfated fucose. Here, we report the identification of Sam10 as an unprecedented fucose-specific sulfotransferase through genetic studies, in vitro reconstitution, and structural analysis, establishing its role in saccharomicin sulfation. Comparative bioassays revealed that sulfation contributes to antibacterial potency, including activity against diverse multidrug-resistant pathogens. We also characterized Sam35 as an efficient adenylyl-sulfate kinase that boosts cellular 3′-phosphoadenosine-5′-phosphate sulfate (PAPS) supply. Our findings define the biochemical and structural basis of saccharomicin sulfation and provide enzymatic tools for engineering novel sulfated oligosaccharide antibiotics.

JACS Au
Extreme Networks (United States) (US), Shanghai Jiao Tong University (CN), Chinese Academy of Sciences (CN), Fudan University (CN), Northwest Institute of Eco-Environment and Resources (CN), Ecologie microbienne (FR), Chemical Synthesis Lab (SG), Imperial College London (GB), Jiangxi Normal University (CN)
Imperial College London, National Natural Science Foundation of China, Chinese Academy of Sciences, Shanghai Jiao Tong University, Chengdu University of Traditional Chinese Medicine, State Key Laboratory of Microbial Metabolism, Jiangxi Normal University, Jiangxi University of Traditional Chinese Medicine, Chengdu University, National Key Research and Development Program of China
Openalex Percentile: Top 9%
Carbohydrate Chemistry and Synthesis
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