ArticleProceedings of the National Academy of Sciences of the United States of America2015
Computational protein design enables a novel one-carbon assimilation pathway.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
120 citing papers in PubMed.
- Engineering of fructose-6-phosphate aldolase for one-carbon conversion to mannitol in a designed biotransformation system.Synthetic and systems biotechnology · 2026Article
- Towards an enzyme cascade synthesis of the bulk chemical acrylic acid.Nature communications · 2026Article
- Process-integrated engineered resting cells for biocatalytic production of rare natural sugars from sole methanol molecules.Nature communications · 2026Article
- Repair of DNA and protein damages caused by formaldehyde improves methanol assimilation.Fundamental research · 2026Article
- Elucidating the catalytic mechanism of a previously undescribed carbohydrate esterase family 7 acetyl xylan esterase (LaCE7A).The FEBS journal · 2026Article
- C2α-carbanion-protonating glutamate discloses tradeoffs between substrate accommodation and reaction rate in actinobacterial 2-hydroxyacyl-CoA lyase.FEBS open bio · 2026Article
- Plug-and-play - enzymatic amino acid production from methanol and carbon dioxide.Nature communications · 2026Article
- FormatotrophicSynthetic and systems biotechnology · 2026Article
- Perspectives for Advancing Biotechnological Succinic Acid Production.Microbial biotechnology · 2026Review
- 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
- Formaldehyde and its surrogates as a C1 platform for defossilised modern societies.Chemical Society reviews · 2025Review
- A blueprint for designing the next-generation of synthetic CNature communications · 2025Review
- Improvement of Soluble Expression, Stability, and Activity of Acetaldehyde Lyase by Elastin-like Polypeptides Fusion for Acetoin Production from Acetaldehyde.Biomolecules · 2025Article
- Industrial applicability of enzymatic and whole-cell processes for the utilization of C1 building blocks.Nature communications · 2025Review
- Carbon sequestration pathways in microorganisms: Advances, strategies, and applications.Engineering microbiology · 2025Review
- Design and implementation of aerobic and ambient CONature communications · 2025Article
- Cell-Free Systems to Mimic and Expand Metabolism.ACS synthetic biology · 2025Review
- Seven critical challenges in synthetic one-carbon assimilation and their potential solutions.FEMS microbiology reviews · 2025Review
- Cell-Free Gene Expression: Methods and Applications.Chemical reviews · 2025Review
60 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
Authors and funding
18 authors.
Funding
Abstract
We describe a computationally designed enzyme, formolase (FLS), which catalyzes the carboligation of three one-carbon formaldehyde molecules into one three-carbon dihydroxyacetone molecule. The existence of FLS enables the design of a new carbon fixation pathway, the formolase pathway, consisting of a small number of thermodynamically favorable chemical transformations that convert formate into a three-carbon sugar in central metabolism. The formolase pathway is predicted to use carbon more efficiently and with less backward flux than any naturally occurring one-carbon assimilation pathway. When supplemented with enzymes carrying out the other steps in the pathway, FLS converts formate into dihydroxyacetone phosphate and other central metabolites in vitro. These results demonstrate how modern protein engineering and design tools can facilitate the construction of a completely new biosynthetic pathway.
Indexed as
Identifiers
What OpenQuestion holds
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.