ArticleJournal of bacteriology2012
Fatty acid biosynthesis in Pseudomonas aeruginosa is initiated by the FabY class of β-ketoacyl acyl carrier protein synthases.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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38 citing papers in PubMed, 71 citations in OpenAlex.
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- Elucidating the functions of fabF1 and fabF2 in Pseudomonas aeruginosa: implications for fatty acid metabolism and pathogenicity.BMC microbiology · 2026Article
- Attenuated Strains of Pseudomonas aeruginosa: A Promising Cell Factory for Rhamnolipid Production.Microbial biotechnology · 2025Review
- The fatty acid synthesis geneMicrobiology spectrum · 2025Article
- SCO6564, a novel 3-ketoacyl acyl carrier protein synthase III, contributes in fatty acid synthesis in Streptomyces coelicolor.PloS one · 2025Article
- An atypical 3-ketoacyl ACP synthase III required for acyl homoserine lactone synthesis inApplied and environmental microbiology · 2024Article
- Direct prediction of antimicrobial resistance inFrontiers in microbiology · 2024Article
- Metabolomics responses and tolerance of Pseudomonas aeruginosa under acoustic vibration stress.PloS one · 2024Article
- Biosynthesis and Gene Regulation of Rhamnolipid Congeners.Current microbiology · 2023Review
- Functional Annotation of Hypothetical Proteins From theBioinformatics and biology insights · 2022Article
- Malonyl-acyl carrier protein decarboxylase activity promotes fatty acid and cell envelope biosynthesis in Proteobacteria.The Journal of biological chemistry · 2021Article
- Effective Disposal of Methylene Blue and Bactericidal Benefits of Using GO-Doped MnOACS omega · 2021Article
- Structural comparison of Acinetobacter baumannii β-ketoacyl-acyl carrier protein reductases in fatty acid and aryl polyene biosynthesis.Scientific reports · 2021Article
- Bacterial lyso-form lipoproteins are synthesized via an intramolecular acyl chain migration.The Journal of biological chemistry · 2020Article
- The Temperature-Regulation ofFrontiers in microbiology · 2020Article
- Mutations ReducingAntimicrobial agents and chemotherapy · 2019Article
- Characterization of 3-Oxacyl-Acyl Carrier Protein Reductase Homolog Genes inFrontiers in microbiology · 2019Article
- Differences in substrate specificity of V. cholerae FabH enzymes suggest new approaches for the development of novel antibiotics and biofuels.The FEBS journal · 2018Article
- Bacterial fatty acid metabolism in modern antibiotic discovery.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- A Genetic Screen Reveals Novel Targets to RenderFrontiers in cellular and infection microbiology · 2017Article
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No grant is acknowledged in the PubMed record.
Abstract
The prototypical type II fatty acid synthesis (FAS) pathway in bacteria utilizes two distinct classes of β-ketoacyl synthase (KAS) domains to assemble long-chain fatty acids, the KASIII domain for initiation and the KASI/II domain for elongation. The central role of FAS in bacterial viability and virulence has stimulated significant effort toward developing KAS inhibitors, particularly against the KASIII domain of the β-acetoacetyl-acyl carrier protein (ACP) synthase FabH. Herein, we show that the opportunistic pathogen Pseudomonas aeruginosa does not utilize a FabH ortholog but rather a new class of divergent KAS I/II enzymes to initiate the FAS pathway. When a P. aeruginosa cosmid library was used to rescue growth in a fabH downregulated strain of Escherichia coli, a single unannotated open reading frame, PA5174, complemented fabH depletion. While deletion of all four KASIII domain-encoding genes in the same P. aeruginosa strain resulted in a wild-type growth phenotype, deletion of PA5174 alone specifically attenuated growth due to a defect in de novo FAS. Siderophore secretion and quorum-sensing signaling, particularly in the rhl and Pseudomonas quinolone signal (PQS) systems, was significantly muted in the absence of PA5174. The defect could be repaired by intergeneric complementation with E. coli fabH. Characterization of recombinant PA5174 confirmed a preference for short-chain acyl coenzyme A (acyl-CoA) substrates, supporting the identification of PA5174 as the predominant enzyme catalyzing the condensation of acetyl coenzyme A with malonyl-ACP in P. aeruginosa. The identification of the functional role for PA5174 in FAS defines the new FabY class of β-ketoacyl synthase KASI/II domain condensation enzymes.
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