ArticleAngewandte Chemie (International ed. in English)2019
Modifying the Thioester Linkage Affects the Structure of the Acyl Carrier Protein.
Article in Angewandte Chemie (International ed. in English), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 21 citations in OpenAlex.
- Photoreactive Pantetheinyl Mimics Reveal Design Limitations for Crypto-Acyl Carrier Proteins.Chembiochem : a European journal of chemical biology · 2026Article
- Preparation and characterization of a iRGD-modified recombinant spider silk particles for antitumor polypeptide drug delivery into cancer cells.BMC biotechnology · 2025Article
- Thioesters Support Efficient Protein Biosynthesis by the Ribosome.ACS central science · 2025Article
- Quantitative Characterization of Chain-Flipping of Acyl Carrier Protein ofJournal of the American Chemical Society · 2024Article
- Using NMR Titration Experiments to Study E. coli FAS-II- and AcpP-Mediated Protein-Protein Interactions.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Control of Unsaturation inBiochemistry · 2022Article
- Atomistic insight on structure and dynamics of spinach acyl carrier protein with substrate length.Biophysical journal · 2021Article
- Structure and mechanistic analyses of the gating mechanism of elongating ketosynthases.ACS catalysis · 2021Article
- Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity.Nature communications · 2021Article
- Decoding allosteric regulation by the acyl carrier protein.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Elucidation of transient protein-protein interactions within carrier protein-dependent biosynthesis.Communications biology · 2021Article
- Structural Characterization of an ACP fromInternational journal of molecular sciences · 2020Article
- Article
- Probing the structure and function of acyl carrier proteins to unlock the strategic redesign of type II polyketide biosynthetic pathways.The Journal of biological chemistryReview
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
At the center of many complex biosynthetic pathways, the acyl carrier protein (ACP) shuttles substrates to appropriate enzymatic partners to produce fatty acids and polyketides. Carrier proteins covalently tether their cargo via a thioester linkage to a phosphopantetheine cofactor. Due to the labile nature of this linkage, chemoenzymatic methods have been developed that involve replacement of the thioester with a more stable amide or ester bond. We explored the importance of the thioester bond to the structure of the carrier protein by using solution NMR spectroscopy and molecular dynamics simulations. Remarkably, the replacement of sulfur with other heteroatoms results in significant structural changes, thus suggesting more rigorous selections of isosteric substitutes is needed.
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