Repurposing the 3-Isocyanobutanoic Acid Adenylation Enzyme SfaB for Versatile Amidation and Thioesterification
Repurposing the 3-Isocyanobutanoic Acid Adenylation Enzyme SfaB for Versatile Amidation and Thioesterification
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重新利用 3-异氰基丁酸腺苷酸化酶 SfaB 进行多功能酰胺化和硫酯化
DOI：
10.1002/anie.202010042
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发表时间：
2021
期刊：
影响因子：
--
通讯作者：
Jing He
中科院分区：
文献类型：
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作者：
Mengyi Zhu;Lijuan Wang;Jing He
Genome mining of microbial natural products enables chemists not only to discover the bioactive molecules with novel skeletons, but also to identify the enzymes that catalyze diverse chemical reactions. Exploring the substrate promiscuity and catalytic mechanism of those biosynthetic enzymes facilitates the development of potential biocatalysts. SfaB is an acyl adenylate‐forming enzyme that adenylates a unique building block, 3‐isocyanobutanoic acid, in the biosynthetic pathway of the diisonitrile natural product SF2768 produced byStreptomyces thioluteus, and this AMP‐ligase was demonstrated to accept a broad range of short‐chain fatty acids (SCFAs). Herein, we repurpose SfaB to catalyze amidation or thioesterification between those SCFAs and various amine or thiol nucleophiles, thereby providing an alternative enzymatic approach to prepare the corresponding amides and thioesters in vitro.
