ArticleOrganic & biomolecular chemistry2019
Active site labeling of fatty acid and polyketide acyl-carrier protein transacylases.
Article in Organic & biomolecular chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Visualizing the Interface of Biotin and Fatty Acid Biosynthesis through SuFEx Probes.Journal of the American Chemical Society · 2024Article
- Structure and mechanistic analyses of the gating mechanism of elongating ketosynthases.ACS catalysis · 2021Article
- Interfacial plasticity facilitates high reaction rate ofProceedings of the National Academy of Sciences of the United States of America · 2020Article
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Authors and funding
3 authors.
Funding
Abstract
Metabolic engineering of fatty acids and polyketides remains challenging due to unresolved protein-protein interactions that are essential to synthase activity. While several chemical probes have been developed to capture and visualize protein interfaces in these systems, acyl carrier protein (ACP) transacylase (AT) domains remain elusive. Herein, we combine a mutational strategy with fluorescent probe design to expedite the study of AT domains from fatty acid and polyketide synthases. We describe the design and evaluation of inhibitor-inspired and substrate-mimetic reporters containing sulfonyl fluoride and β-lactone warheads. Moreover, specific active-site labeling occurs by optimizing pH, time, and probe concentration, and selective labeling is achieved in the presence of inhibitors of competing domains. These findings provide a panel of AT-targeting probes and set the stage for future combinatorial biosynthetic and drug discovery initiatives.
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