ArticleNature communications2016
A crotonyl-CoA reductase-carboxylase independent pathway for assembly of unusual alkylmalonyl-CoA polyketide synthase extender units.
Article in Nature communications, 2016. 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, 31 citations in OpenAlex.
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- Enhanced triacylglycerol metabolism contributes to the efficient biosynthesis of spinosad inSynthetic and systems biotechnology · 2024Article
- NLRP10 promotes AGEs-induced NLRP1 and NLRP3 inflammasome activation via ROS/MAPK/NF-κB signaling in human periodontal ligament cells.Odontology · 2024Article
- Enhancing armeniaspirols production through multi-level engineering of a native Streptomyces producer.Microbial cell factories · 2023Article
- Development of a Pantetheine Force Field Library for Molecular Modeling.Journal of chemical information and modeling · 2021Article
- Structural and functional comparison of Saccharomonospora azurea strains in terms of primycin producing ability.World journal of microbiology & biotechnology · 2020Article
- The biosynthetic pathway to ossamycin, a macrocyclic polyketide bearing a spiroacetal moiety.PloS one · 2019Article
- Acyltransferases as Tools for Polyketide Synthase Engineering.Antibiotics (Basel, Switzerland) · 2018Review
- Searching for Glycosylated Natural Products in Actinomycetes and Identification of Novel Macrolactams and Angucyclines.Frontiers in microbiology · 2018Article
- Engineered polyketides: Synergy between protein and host level engineering.Synthetic and systems biotechnology · 2017Review
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
Abstract
Type I modular polyketide synthases assemble diverse bioactive natural products. Such multienzymes typically use malonyl and methylmalonyl-CoA building blocks for polyketide chain assembly. However, in several cases more exotic alkylmalonyl-CoA extender units are also known to be incorporated. In all examples studied to date, such unusual extender units are biosynthesized via reductive carboxylation of α, β-unsaturated thioesters catalysed by crotonyl-CoA reductase/carboxylase (CCRC) homologues. Here we show using a chemically-synthesized deuterium-labelled mechanistic probe, and heterologous gene expression experiments that the unusual alkylmalonyl-CoA extender units incorporated into the stambomycin family of polyketide antibiotics are assembled by direct carboxylation of medium chain acyl-CoA thioesters. X-ray crystal structures of the unusual β-subunit of the acyl-CoA carboxylase (YCC) responsible for this reaction, alone and in complex with hexanoyl-CoA, reveal the molecular basis for substrate recognition, inspiring the development of methodology for polyketide bio-orthogonal tagging via incorporation of 6-azidohexanoic acid and 8-nonynoic acid into novel stambomycin analogues.
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