ArticleNature communications2025
Pseudomonas aeruginosa acyl-CoA dehydrogenases and structure-guided inversion of their substrate specificity.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- An extragenic fix for a broken enzyme.Microbiology (Reading, England) · 2026Article
- Distinctive Lacritin Cleavage-Potentiated Bactericidal Alteration of thebioRxiv : the preprint server for biology · 2026Article
- L-cysteine inhibited the growth ofApplied and environmental microbiology · 2026Article
- ProtPen combines sequence- and structure-based approaches to facilitate protein function predictions on a proteome-wide scale.bioRxiv : the preprint server for biology · 2026Article
- Paving the way or sharing goods?-Interactions between pairs ofFrontiers in microbiology · 2026Article
- An allantoin-inducible glyoxylate utilization pathway inMicrobiology (Reading, England) · 2025Article
- Pathogenicity and virulence ofVirulence · 2025Review
- Genome-wide evolutionary selection pressures acting onNAR molecular medicine · 2025Article
- Multidimensional Research on Hair Loss in Young Chinese Females With Oily Scalps.Journal of cosmetic dermatology · 2025Article
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Authors and funding
13 authors.
Funding
Abstract
Fatty acids are a primary source of carbon for Pseudomonas aeruginosa (PA) in the airways of people with cystic fibrosis (CF). Here, we use tandem mass-tag proteomics to analyse the protein expression profile of a CF clinical isolate grown on different fatty acids. Two fatty acyl-CoA dehydrogenases (designated FadE1 and FadE2) are strongly induced during growth on fatty acids. FadE1 displays a strong preference for long-chain acyl-CoAs, whereas FadE2 exclusively utilizes medium-chain acyl-CoAs. Structural analysis of the enzymes enables us to identify residues comprising the substrate selectivity filter in each. Engineering these residues enables us to invert the substrate specificity of each enzyme. Mutants in fadE1 displayed impaired virulence in an infection model, and decreased growth on long chain fatty acids. The unique features of the substrate binding pocket enable us to identify an inhibitor that is differentially active against FadE1 and FadE2.
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