ArticleApplied and environmental microbiology2014
Functional screening and in vitro analysis reveal thioesterases with enhanced substrate specificity profiles that improve short-chain fatty acid production in Escherichia coli.
Article in Applied and environmental microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.
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Who cites it
28 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Regulation of Intestinal Inflammation by Dietary Fats.Frontiers in immunology · 2020Pooled it
- Molecular Chain Elongation Mechanism for n-Caproate Biosynthesis by Megasphaera Hexanoica.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Engineering thioesterase as a driving force for novel itaconate production via its degradation scheme.Metabolic engineering communications · 2024Article
- Citrate synthase variants improve yield of acetyl-CoA derived 3-hydroxybutyrate in Escherichia coli.Microbial cell factories · 2024Article
- Overcoming barriers to medium-chain fatty alcohol production.Current opinion in biotechnology · 2024Review
- A strategy to enhance and modify fatty acid synthesis in Corynebacterium glutamicum and Escherichia coli: overexpression of acyl-CoA thioesterases.Microbial cell factories · 2023Article
- Relative Activities of the β-ketoacyl-CoA and Acyl-CoA Reductases Influence Product Profile and Flux in a Reversed β-Oxidation Pathway.ACS catalysis · 2023Article
- Escherichia coli YigI is a Conserved Gammaproteobacterial Acyl-CoA Thioesterase Permitting Metabolism of Unusual Fatty Acid Substrates.Journal of bacteriology · 2022Article
- Reverse β-oxidation pathways for efficient chemical production.Journal of industrial microbiology & biotechnology · 2022Article
- Metabolic engineering strategies to produce medium-chain oleochemicals via acyl-ACP:CoA transacylase activity.Nature communications · 2022Article
- Physiological activity of E. coli engineered to produce butyric acid.Microbial biotechnology · 2022Article
- Thioesterase enzyme families: Functions, structures, and mechanisms.Protein science : a publication of the Protein Society · 2022Article
- Mucor circinelloides: a model organism for oleaginous fungi and its potential applications in bioactive lipid production.Microbial cell factories · 2022Review
- A kinetic rationale for functional redundancy in fatty acid biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Increased Accumulation of Medium-Chain Fatty Acids by Dynamic Degradation of Long-Chain Fatty Acids inGenes · 2020Article
- In vitro prototyping and rapid optimization of biosynthetic enzymes for cell design.Nature chemical biology · 2020Article
- Biosynthetic engineering of the antifungal, anti-MRSA auroramycin.Microbial cell factories · 2020Article
- Effect of a Novel Alpha/Beta Hydrolase Domain Protein on Tolerance ofFrontiers in bioengineering and biotechnology · 2020Article
- Beyond Intracellular Accumulation of Polyhydroxyalkanoates: Chiral Hydroxyalkanoic Acids and Polymer Secretion.Frontiers in bioengineering and biotechnology · 2020Review
- Comparison of engineered Escherichia coli AF1000 and BL21 strains for (R)-3-hydroxybutyrate production in fed-batch cultivation.Applied microbiology and biotechnology · 2019Article
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2 authors.
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Abstract
Short-chain fatty acid (SCFA) biosynthesis is pertinent to production of biofuels, industrial compounds, and pharmaceuticals from renewable resources. To expand on Escherichia coli SCFA products, we previously implemented a coenzyme A (CoA)-dependent pathway that condenses acetyl-CoA to a diverse group of short-chain fatty acyl-CoAs. To increase product titers and reduce premature pathway termination products, we conducted in vivo and in vitro analyses to understand and improve the specificity of the acyl-CoA thioesterase enzyme, which releases fatty acids from CoA. A total of 62 putative bacterial thioesterases, including 23 from the cow rumen microbiome, were inserted into a pathway that condenses acetyl-CoA to an acyl-CoA molecule derived from exogenously provided propionic or isobutyric acid. Functional screening revealed thioesterases that increase production of saturated (valerate), unsaturated (trans-2-pentenoate), and branched (4-methylvalerate) SCFAs compared to overexpression of E. coli thioesterase tesB or native expression of endogenous thioesterases. To determine if altered thioesterase acyl-CoA substrate specificity caused the increase in product titers, six of the most promising enzymes were analyzed in vitro. Biochemical assays revealed that the most productive thioesterases rely on promiscuous activity but have greater specificity for product-associated acyl-CoAs than for precursor acyl-CoAs. In this study, we introduce novel thioesterases with improved specificity for saturated, branched, and unsaturated short-chain acyl-CoAs, thereby expanding the diversity of potential fatty acid products while increasing titers of current products. The growing uncertainty associated with protein database annotations denotes this study as a model for isolating functional biochemical pathway enzymes in situations where experimental evidence of enzyme function is absent.
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