ArticleNature communications2015
Redox-switch regulatory mechanism of thiolase from Clostridium acetobutylicum.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Reverse beta-oxidation for biochemical production: insights into the functional properties of key enzymes.BMB reports · 2026Review
- EngineeringACS synthetic biology · 2026Article
- Classification of Protein Disulfide Bonds.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Molecular Chain Elongation Mechanism for n-Caproate Biosynthesis by Megasphaera Hexanoica.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Enhancing the activity and succinyl-CoA specificity of 3-ketoacyl-CoA thiolase Tfu_0875 through rational binding pocket engineering.Synthetic and systems biotechnology · 2024Article
- Microbial Cell Factories in the Bioeconomy Era: From Discovery to Creation.Biodesign research · 2024Review
- The potential of native and engineered Clostridia for biomass biorefining.Frontiers in bioengineering and biotechnology · 2024Review
- Harnessing redox proteomics to study metabolic regulation and stress response in lignin-fed Rhodococci.Biotechnology for biofuels and bioproducts · 2023Article
- Gut microbial metabolism of 5-ASA diminishes its clinical efficacy in inflammatory bowel disease.Nature medicine · 2023Article
- NADH-based kinetic model for acetone-butanol-ethanol production byFrontiers in bioengineering and biotechnology · 2023Article
- Integrated omics approach to unveil antifungal bacterial polyynes as acetyl-CoA acetyltransferase inhibitors.Communications biology · 2022Article
- Article
- The 3-ketoacyl-CoA thiolase: an engineered enzyme for carbon chain elongation of chemical compounds.Applied microbiology and biotechnology · 2020Review
- Aspergillus fumigatus Mitochondrial Acetyl Coenzyme A Acetyltransferase as an Antifungal Target.Applied and environmental microbiology · 2020Article
- Article
- Pathway dissection, regulation, engineering and application: lessons learned from biobutanol production by solventogenic clostridia.Biotechnology for biofuels · 2020Review
- Allosteric disulphide bonds as reversible mechano-sensitive switches that control protein functions in the vasculature.Biophysical reviews · 2019Review
- Constructing a synthetic pathway for acetyl-coenzyme A from one-carbon through enzyme design.Nature communications · 2019Article
- Co-production of solvents and organic acids in butanol fermentation byRSC advances · 2019Article
- Allosteric disulfides: Sophisticated molecular structures enabling flexible protein regulation.The Journal of biological chemistry · 2019Review
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thiolase is the first enzyme catalysing the condensation of two acetyl-coenzyme A (CoA) molecules to form acetoacetyl-CoA in a dedicated pathway towards the biosynthesis of n-butanol, an important solvent and biofuel. Here we elucidate the crystal structure of Clostridium acetobutylicum thiolase (CaTHL) in its reduced/oxidized states. CaTHL, unlike those from other aerobic bacteria such as Escherichia coli and Zoogloea ramegera, is regulated by the redox-switch modulation through reversible disulfide bond formation between two catalytic cysteine residues, Cys88 and Cys378. When CaTHL is overexpressed in wild-type C. acetobutylicum, butanol production is reduced due to the disturbance of acidogenic to solventogenic shift. The CaTHL(V77Q/N153Y/A286K) mutant, which is not able to form disulfide bonds, exhibits higher activity than wild-type CaTHL, and enhances butanol production upon overexpression. On the basis of these results, we suggest that CaTHL functions as a key enzyme in the regulation of the main metabolism of C. acetobutylicum through a redox-switch regulatory mechanism.
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