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Updated: Mar 18, 2026

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
Published on: October 2, 2018
Diiron Monooxygenase Complex Involved in Antimycin Biosynthesis Transforms Anthraniloyl Thioester into 3-Aminosalicyl
Yuqiong Zhao1, Takayoshi Awakawa2, Ikuro Abe2
1State Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, University of Chinese Academy of Sciences, 345 Lingling Road, Shanghai 200032, China.
Abstract:
Antimycins feature a nine-membered dilactone core and a bioactivity-essential 3-formaminosalic acid. Herein, we demonstrate that the formation of 3-aminosalicylate is catalyzed by AntHIJKL, a multicomponent diiron monooxygenase complex, via an unusual carrier protein-dependent oxidative rearrangement. AntH and AntJ constitute the minimal catalytic unit to convert anthraniloyl thioester into 3-aminosalicyl thioester on the carrier protein AntG, while AntI, AntK, and AntL function as auxiliary redox partners. This study expands the functional scope of multicomponent diiron monooxygenases.
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