ArticleACS synthetic biology2018
Highly Active C
Article in ACS synthetic biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
32 citing papers in PubMed, 85 citations in OpenAlex.
- Engineering Escherichia coli to produce medium chain oleochemicals from C2 substrates.Journal of industrial microbiology & biotechnology · 2026Article
- A synthetic metabolic pathway for the de novo biosynthesis of medium chain length γ- and δ-lactones.Journal of biological engineering · 2025Article
- A metabolic engineering strategy for producing poly-(3-hydroxyoctanoic acid) in Escherichia coli from glycerol.Metabolic engineering · 2025Article
- Concentration-Dependent CsrA Regulation of theACS synthetic biology · 2025Article
- A Fast-Pass, Desorption Electrospray Ionization Mass Spectrometry Strategy for Untargeted Metabolic Phenotyping.Journal of the American Society for Mass Spectrometry · 2025Article
- Genome reduction improves octanoic acid production in scale down bioreactors.Microbial biotechnology · 2024Article
- Rewiring native post-transcriptional global regulators to achieve designer, multi-layered genetic circuits.Nature communications · 2024Article
- Pseudomonas putida as a platform for medium-chain length α,ω-diol production: Opportunities and challenges.Microbial biotechnology · 2024Article
- Overcoming barriers to medium-chain fatty alcohol production.Current opinion in biotechnology · 2024Review
- Light-inducible protein degradation ineLife · 2024Article
- Machine learning model of the catalytic efficiency and substrate specificity of acyl-ACP thioesterase variants generated from natural andFrontiers in bioengineering and biotechnology · 2024Article
- A strategy to enhance and modify fatty acid synthesis in Corynebacterium glutamicum and Escherichia coli: overexpression of acyl-CoA thioesterases.Microbial cell factories · 2023Article
- Longitudinal Single-Cell Imaging of Engineered Strains with Stimulated Raman Scattering to Characterize Heterogeneity in Fatty Acid Production.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 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
- CsrA Shows Selective Regulation of sRNA-mRNA Networks.bioRxiv : the preprint server for biology · 2023Article
- An optogenetic toolkit for light-inducible antibiotic resistance.Nature communications · 2023Article
- Determinants of substrate specificity in a catalytically diverse family of acyl-ACP thioesterases from plants.BMC plant biology · 2023Article
- CsrA selectively modulates sRNA-mRNA regulator outcomes.Frontiers in molecular biosciences · 2023Article
- A kinetic framework for modeling oleochemical biosynthesis in Escherichia coli.Biotechnology and bioengineering · 2022Article
- Metabolic engineering strategies to produce medium-chain oleochemicals via acyl-ACP:CoA transacylase activity.Nature communications · 2022Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Microbial metabolism is an attractive route for producing medium chain length fatty acids, e.g., octanoic acid, used in the oleochemical industry. One challenge to this strategy is the lack of enzymes that are both highly active in a microbial host and selective toward substrates with desired chain length. Of the many steps in fatty acid biosynthesis, the thioesterase is the most widely used enzyme for controlling chain length. Thioesterases hydrolyze the thioester bond between fatty acids and the acyl-carrier protein (ACP) or coenzyme A (CoA) cofactor. The functional role of thioesterases varies between organisms ( i.e., bacteria vs plant) and therefore so do the substrate specificities. As a result, microbial biocatalysts that utilize a heterologous thioesterase either produce high titers of fatty acids with mixed chain lengths or low titers of products with a narrow chain length distribution. To search for highly active enzymes that selectively hydrolyze octanoyl-ACP, we developed a genetic selection based on the lipoic acid requirement of Escherichia coli. We used the selection to identify variants in a randomly mutagenized library of the C
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.