ArticleJournal of the American Chemical Society2018
An Oxetane-Based Polyketide Surrogate To Probe Substrate Binding in a Polyketide Synthase.
Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 32 citations in OpenAlex.
- Do Amino-Oxetanes Resemble Amides? A Matched Molecular Pairs Property and Structural Comparison.Journal of medicinal chemistry · 2026Article
- Elucidating the Iterative Elongation Mechanism in a Type III Polyketide Synthase.Journal of the American Chemical Society · 2025Article
- Oxetanes in Drug Discovery Campaigns.Journal of medicinal chemistry · 2023Review
- Activity of Fatty Acid Biosynthesis Initiating Ketosynthase FabH with Acetyl/Malonyl-oxa/aza(dethia)CoAs.ACS chemical biology · 2023Article
- Unexpected Isomerization of Oxetane-Carboxylic Acids.Organic letters · 2022Article
- Article
- Enzymology of standalone elongating ketosynthases.Chemical science · 2022Review
- A Light-Activated Acyl Carrier Protein "Trap" for Intermediate Capture in Type II Iterative Polyketide Biocatalysis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019Article
- Robustness and Efficiency of Poisson-Boltzmann Modeling on Graphics Processing Units.Journal of chemical information and modeling · 2019Article
- Computational structural enzymology methodologies for the study and engineering of fatty acid synthases, polyketide synthases and nonribosomal peptide synthetases.Methods in enzymology · 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
- 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
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
Abstract
Polyketides are a large class of bioactive natural products with a wide range of structures and functions. Polyketides are biosynthesized by large, multidomain enzyme complexes termed polyketide synthases (PKSs). One of the primary challenges when studying PKSs is the high reactivity of their poly-β-ketone substrates. This has hampered structural and mechanistic characterization of PKS-polyketide complexes, and, as a result, little is known about how PKSs position the unstable substrates for proper catalysis while displaying high levels of regio- and stereospecificity. As a first step toward a general plan to use oxetanes as carbonyl isosteres to broadly interrogate PKS chemistry, we describe the development and application of an oxetane-based PKS substrate mimic. This enabled the first structural determination of the acyl-enzyme intermediate of a ketosynthase (KS) in complex with an inert extender unit mimic. The crystal structure, in combination with molecular dynamics simulations, led to a proposed mechanism for the unique activity of DpsC, the priming ketosynthase for daunorubicin biosynthesis. The successful application of an oxetane-based polyketide mimic suggests that this novel class of probes could have wide-ranging applications to the greater biosynthetic community interested in the mechanistic enzymology of iterative PKSs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.