ArticleBiochemistry2022
Multiple Functions of the Type II Thioesterase Associated with the Phoslactomycin Polyketide Synthase.
Article in Biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Structure-Activity Relationship of Cycling Molecular Assemblies for Golgi Targeting and Disruption.Journal of medicinal chemistry · 2026Article
- Charting the Biosynthetic Landscape of Hybrid Polyketide-Nonribosomal Peptide-Specialized Lipids.JACS Au · 2026Article
- Covalent warhead assembly in fostriecin biosynthesis involves malonylation-lactonisation by a bifunctional thioesterase and enzymatic demalonylation.Nature communications · 2026Article
- Genetic analysis of pigment production in the fungus Exophiala dermatitidis mutant strains obtained via nontargeted UV mutagenesis.G3 (Bethesda, Md.) · 2025Article
- Metabolic engineering ofSynthetic and systems biotechnology · 2025Article
- Refactoring the pikromycin synthase for the modular biosynthesis of macrolide antibiotics in E. coli.Research square · 2025Article
- Substrate Trapping in Polyketide Synthase Thioesterase Domains: Structural Basis for Macrolactone Formation.ACS catalysis · 2024Article
- An oxidoreductase gene CtnD involved in citrinin biosynthesis in Monascus purpureus verified by CRISPR/Cas9 gene editing and overexpression.Mycotoxin research · 2023Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Polyketide synthases (PKSs) are molecular assembly lines that condense basic chemical building blocks for the production of structurally diverse polyketides. Many PKS biosynthetic gene clusters contain a gene encoding for a type II thioesterase (TEII). It is believed that TEIIs exert a proofreading function and restore or increase the productivity of PKSs by removing aberrant modifications on the acyl-carrier proteins (ACPs) of the PKS assembly line. Yet biochemical evidence is still sparse. Here, we investigated the function of PnG, the TEII of the phoslactomycin PKS (Pn PKS), in the context of its cognate assembly line
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