ArticleNature chemical biology2019
2-Hydroxyacyl-CoA lyase catalyzes acyloin condensation for one-carbon bioconversion.
Article in Nature chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 91 citations in OpenAlex.
- Reprogramming energy system for growth and bioproduction from CO₂ and methanol in Escherichia coli.Nature communications · 2026Article
- Towards an enzyme cascade synthesis of the bulk chemical acrylic acid.Nature communications · 2026Article
- Repair of DNA and protein damages caused by formaldehyde improves methanol assimilation.Fundamental research · 2026Article
- Advances in synthetic biology for engineering methylotrophic microbial cell factories.Journal of bacteriology · 2026Review
- N-Heterocyclic Carbene (NHC) Catalysis in Enzymatic Organic Synthesis.Coordination chemistry reviews · 2026Article
- Design and implementation of aerobic and ambient CONature communications · 2025Article
- A synthetic methylotroph achieves accelerated cell growth by alleviating transcription-replication conflicts.Nature communications · 2025Article
- Concatenating Microbial, Enzymatic, and Organometallic Catalysis for Integrated Conversion of Renewable Carbon Sources.JACS Au · 2024Review
- A synthetic cell-free pathway for biocatalytic upgrading of one-carbon substrates.bioRxiv : the preprint server for biology · 2024Article
- Revealing reaction intermediates in one-carbon elongation by thiamine diphosphate/CoA-dependent enzyme family.Communications chemistry · 2024Article
- The Weight of Bariatric Surgery: Wernicke-Korsakoff Syndrome after Vertical Sleeve Gastrectomy-A Case Series.Journal of personalized medicine · 2024Article
- Constructing efficient bacterial cell factories to enable one-carbon utilization based on quantitative biology: A review.Quantitative biology (Beijing, China) · 2024Review
- Engineering a synthetic energy-efficient formaldehyde assimilation cycle in Escherichia coli.Nature communications · 2023Article
- Artificial multi-enzyme cascades and whole-cell transformation for bioconversion of C1 compounds: Advances, challenge and perspectives.Synthetic and systems biotechnology · 2023Review
- Metabolic engineering strategies for microbial utilization of methanol.Engineering microbiology · 2023Review
- Integration of ARTP Mutation and Adaptive Laboratory Evolution to Reveal 1,4-Butanediol Degradation in Pseudomonas putida KT2440.Microbiology spectrum · 2023Article
- Enzymatic Conversion of COChemical reviews · 2023Review
- Engineering a new-to-nature cascade for phosphate-dependent formate to formaldehyde conversion in vitro and in vivo.Nature communications · 2023Article
- Unravelling Formaldehyde Metabolism in Bacteria: Road towards Synthetic Methylotrophy.Microorganisms · 2022Review
- Developing methylotrophic microbial platforms for a methanol-based bioindustry.Frontiers in bioengineering and biotechnology · 2022Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Despite the potential of biotechnological processes for one-carbon (C1) bioconversion, efficient biocatalysts required for their implementation are yet to be developed. To address intrinsic limitations of native C1 biocatalysts, here we report that 2-hydroxyacyl CoA lyase (HACL), an enzyme involved in mammalian α-oxidation, catalyzes the ligation of carbonyl-containing molecules of different chain lengths with formyl-coenzyme A (CoA) to produce C1-elongated 2-hydroxyacyl-CoAs. We discovered and characterized a prokaryotic variant of HACL and identified critical residues for this newfound activity, including those supporting the hypothesized thiamine pyrophosphate-dependent acyloin condensation mechanism. The use of formyl-CoA as a C1 donor provides kinetic advantages and enables C1 bioconversion to multi-carbon products, demonstrated here by engineering an Escherichia coli whole-cell biotransformation system for the synthesis of glycolate and 2-hydroxyisobutyrate from formaldehyde and formaldehyde plus acetone, respectively. Our work establishes a new approach for C1 bioconversion and the potential for HACL-based pathways to support synthetic methylotrophy.
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