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Updated: Aug 5, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
Published on: August 1, 2018
The hidden role of thioesterase PltG in pyoluteorin biosynthesis
Li-Ming Luo1, Hang Xu1, Hao-Nan Cao1
1Ministry of Education Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou 730000, China. yanghaojack@lzu.edu.cn.
Abstract:
Thioesterase PltG is demonstrated to restore the pyoluteorin biosynthetic machinery by removing aberrant intermediates that block ACP, a function distinct from its presumed role in cyclization. Furthermore, DFT calculations indicate the chemical feasibility of the proposed spontaneous cyclization from 1-ACP to intermediate A. Together, our findings redefine the physiological role of PltG and advance the mechanistic understanding of pyoluteorin biosynthesis.
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