ReviewMicrobiology and molecular biology reviews : MMBR2004
Microbial type I fatty acid synthases (FAS): major players in a network of cellular FAS systems.
Review in Microbiology and molecular biology reviews : MMBR, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.
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Who cites it
134 citing papers in PubMed, 379 citations in OpenAlex.
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- Structural basis of product recognition by Mycobacterium tuberculosis fatty acid synthase.Protein science : a publication of the Protein Society · 2026Article
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- Serendipity and the Slime Mold: A Visual Survey of High-Molecular-Weight Protein Assemblies Reveals the Structure of the Polyketide Synthase Pks16.Molecular & cellular proteomics : MCP · 2026Article
- Exploring lipid diversity and minimalism to define membrane requirements for synthetic cells.FEBS letters · 2025Review
- Engineering N-acyl-homoserine lactone-based quorum-sensing circuit for dynamic regulatory control in Saccharomyces cerevisiae.Communications biology · 2025Article
- Effect of High-Temperature Stress on Fatty Acid Composition and Undecylprodiginine Biosynthesis inMicroorganisms · 2025Article
- Protein-Protein Complex Stability Controls Substrate Scope in a β-Ketoacyl-ACP Reductase Specific for Medium Chains.Angewandte Chemie (International ed. in English) · 2025Article
- Fatty acid synthase in high and low lipid-producing strains of Mucor circinelloides: identification, phylogenetic analysis, and expression profiling during growth and lipid accumulation.Biotechnology letters · 2025Article
- Sustainable Lipid Production withMicroorganisms · 2025Review
- The role of uncharacterized protein Taf1 in regulating ATP levels and virulence of Cryptococcus neoformans.BMC microbiology · 2025Article
- Engineering of Corynebacterium glutamicum for the synthesis of aromatic compounds.Applied microbiology and biotechnology · 2025Review
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- Preparation of Multifunctional Nano-Protectants for High-Efficiency Green Control of Anthracnose.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Structural and Biochemical Studies on Klebsiella Pneumoniae Enoyl-ACP Reductase (FabI) Suggest Flexible Substrate Binding Site.The protein journal · 2024Article
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- Optimization of a hybrid bacterial/Metabolic engineering communications · 2023Article
74 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The present review focuses on microbial type I fatty acid synthases (FASs), demonstrating their structural and functional diversity. Depending on their origin and biochemical function, multifunctional type I FAS proteins form dimers or hexamers with characteristic organization of their catalytic domains. A single polypeptide may contain one or more sets of the eight FAS component functions. Alternatively, these functions may split up into two different and mutually complementing subunits. Targeted inactivation of the individual yeast FAS acylation sites allowed us to define their roles during the overall catalytic process. In particular, their pronounced negative cooperativity is presumed to coordinate the FAS initiation and chain elongation reactions. Expression of the unlinked genes, FAS1 and FAS2, is in part constitutive and in part subject to repression by the phospholipid precursors inositol and choline. The interplay of the involved regulatory proteins, Rap1, Reb1, Abf1, Ino2/Ino4, Opi1, Sin3 and TFIIB, has been elucidated in considerable detail. Balanced levels of subunits alpha and beta are ensured by an autoregulatory effect of FAS1 on FAS2 expression and by posttranslational degradation of excess FAS subunits. The functional specificity of type I FAS multienzymes usually requires the presence of multiple FAS systems within the same cell. De novo synthesis of long-chain fatty acids, mitochondrial fatty acid synthesis, acylation of certain secondary metabolites and coenzymes, fatty acid elongation, and the vast diversity of mycobacterial lipids each result from specific FAS activities. The microcompartmentalization of FAS activities in type I multienzymes may thus allow for both the controlled and concerted action of multiple FAS systems within the same cell.
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