ArticleChembiochem : a European journal of chemical biology2021
Activation, Structure, Biosynthesis and Bioactivity of Glidobactin-like Proteasome Inhibitors from Photorhabdus laumondii.
Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Heterologous Production of Barnesin A, an NRPS-PKS Hybrid Containing a Rare Vinylogous Arginine Moiety.Chembiochem : a European journal of chemical biology · 2026Article
- A rapid combinatorial assembly method for gene cluster characterisation illuminates glidobactin biosynthesis.Synthetic and systems biotechnology · 2026Article
- ExploringMolecules (Basel, Switzerland) · 2024Review
- Genetic toolbox for Photorhabdus and Xenorhabdus: pSEVA based heterologous expression systems and CRISPR/Cpf1 based genome editing for rapid natural product profiling.Microbial cell factories · 2024Article
- Optical Control of Proteasomal Protein Degradation with a Photoswitchable Lipopeptide.Angewandte Chemie (International ed. in English) · 2024Article
- Comprehensive Structure-Activity Relationship Studies of Cepafungin Enabled by Biocatalytic C-H Oxidations.ACS central science · 2023Article
- Evaluation of the Antifungal Activities ofJournal of fungi (Basel, Switzerland) · 2022Article
- Complex peptide natural products: Biosynthetic principles, challenges and opportunities for pathway engineering.Synthetic and systems biotechnology · 2022Article
- Beyond Soil-Dwelling Actinobacteria: Fantastic Antibiotics and Where to Find Them.Antibiotics (Basel, Switzerland) · 2022Review
- Review
- Activation, Structure, Biosynthesis and Bioactivity of Glidobactin-like Proteasome Inhibitors from Photorhabdus laumondii.Chembiochem : a European journal of chemical biology · 2021Article
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
The glidobactin-like natural products (GLNPs) glidobactin A and cepafungin I have been reported to be potent proteasome inhibitors and are regarded as promising candidates for anticancer drug development. Their biosynthetic gene cluster (BGC) plu1881-1877 is present in entomopathogenic Photorhabdus laumondii but silent under standard laboratory conditions. Here we show the largest subset of GLNPs, which are produced and identified after activation of the silent BGC in the native host and following heterologous expression of the BGC in Escherichia coli. Their chemical diversity results from a relaxed substrate specificity and flexible product release in the assembly line of GLNPs. Crystal structure analysis of the yeast proteasome in complex with new GLNPs suggests that the degree of unsaturation and the length of the aliphatic tail are critical for their bioactivity. The results in this study provide the basis to engineer the BGC for the generation of new GLNPs and to optimize these natural products resulting in potential drugs for cancer therapy.
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