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Modifying the Thioester Linkage Affects the Structure of the Acyl Carrier Protein.
- Source :
- Angewandte Chemie (International ed. in English); vol 58, iss 32, 10888-10892; 1433-7851
- Publication Year :
- 2019
-
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.
Details
- Database :
- OAIster
- Journal :
- Angewandte Chemie (International ed. in English); vol 58, iss 32, 10888-10892; 1433-7851
- Notes :
- Angewandte Chemie (International ed. in English) vol 58, iss 32, 10888-10892 1433-7851
- Publication Type :
- Electronic Resource
- Accession number :
- edsoai.on1287294759
- Document Type :
- Electronic Resource