ArticleJournal of the American Chemical Society2016
Trapping of the Enoyl-Acyl Carrier Protein Reductase-Acyl Carrier Protein Interaction.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Visualizing acyl carrier protein interactions within a crosslinked type I polyketide synthase.Nature communications · 2025Article
- Elucidating the Iterative Elongation Mechanism in a Type III Polyketide Synthase.Journal of the American Chemical Society · 2025Article
- Activity Mapping the Acyl Carrier Protein: Elongating Ketosynthase Interaction in Fatty Acid Biosynthesis.Biochemistry · 2020Article
- Cryo-EM Structures and Regulation of Arabinofuranosyltransferase AftD from Mycobacteria.Molecular cell · 2020Article
- Electron cryomicroscopy observation of acyl carrier protein translocation in type I fungal fatty acid synthase.Scientific reports · 2019Article
- Trapping interactions between catalytic domains and carrier proteins of modular biosynthetic enzymes with chemical probes.Natural product reports · 2018Review
- Type II fatty acid and polyketide synthases: deciphering protein-protein and protein-substrate interactions.Natural product reports · 2018Review
- Inhibitors of protein-protein interactions (PPIs): an analysis of scaffold choices and buried surface area.Current opinion in chemical biology · 2018Review
- Towards Precision Engineering of Canonical Polyketide Synthase Domains: Recent Advances and Future Prospects.Molecules (Basel, Switzerland) · 2017Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
An ideal target for metabolic engineering, fatty acid biosynthesis remains poorly understood on a molecular level. These carrier protein-dependent pathways require fundamental protein-protein interactions to guide reactivity and processivity, and their control has become one of the major hurdles in successfully adapting these biological machines. Our laboratory has developed methods to prepare acyl carrier proteins (ACPs) loaded with substrate mimetics and cross-linkers to visualize and trap interactions with partner enzymes, and we continue to expand the tools for studying these pathways. We now describe application of the slow-onset, tight-binding inhibitor triclosan to explore the interactions between the type II fatty acid ACP from Escherichia coli, AcpP, and its corresponding enoyl-ACP reductase, FabI. We show that the AcpP-triclosan complex demonstrates nM binding, inhibits in vitro activity, and can be used to isolate FabI in complex proteomes.
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Registered trials
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