ArticleNature communications2023
Engineered repeat proteins as scaffolds to assemble multi-enzyme systems for efficient cell-free biosynthesis.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
14 citing papers in PubMed, 51 citations in OpenAlex.
- Sequential Conjugation of Two Different Types of Catalytically Active Enzymes to Liposomes via Bis-Aryl Hydrazone Bonds.ACS omega · 2026Article
- Liquid-Liquid Phase Separation-Enhanced Multienzyme Catalysis: Mechanisms and Applications.ChemSusChem · 2026Review
- Confined Catalysis of Enzymes: Enhancement Strategies, Materials, and Biosensor Applications.Journal of functional biomaterials · 2026Review
- Oppositely Charged Single Enzyme Nanogels Form Versatile Coacervates for Efficient Enzyme Cascade Catalysis.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- A tri-modal contrastive learning framework for protein representation learning.Cell reports methods · 2026Article
- Machine learning-driving optimization and spatial assembly of a cell-free system for high-yield liquiritigenin production.Advanced biotechnology · 2026Article
- Metabolic Engineering ofChem & bio engineering · 2026Article
- Construction of artificial organellesChemical science · 2025Review
- Synthesis, Characterization, and Enzyme Conjugation of Polycaprolactone Nanofibers for Tissue Engineering.Pharmaceutics · 2025Article
- Local structural flexibility drives oligomorphism in computationally designed protein assemblies.Nature structural & molecular biology · 2025Article
- Designer Glycolysomes: Colocalisation of Glycolytic Enzymes on a Cellulosome-Based Synthetic Protein Scaffold.Microbial biotechnology · 2025Article
- Semirational Design of SenC to Enhance Organic Selenium Biosynthesis.Microbial biotechnology · 2025Article
- Programming interchangeable and reversible heterooligomeric protein self-assembly using a bifunctional ligand.Chemical science · 2024Article
- Temperature-Controlled Expression of a Recombinant Human-like Collagen I Peptide inBioengineering (Basel, Switzerland) · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multi-enzymatic cascades with enzymes arranged in close-proximity through a protein scaffold can trigger a substrate channeling effect, allowing for efficient cofactor reuse with industrial potential. However, precise nanometric organization of enzymes challenges the design of scaffolds. In this study, we create a nanometrically organized multi-enzymatic system exploiting engineered Tetrapeptide Repeat Affinity Proteins (TRAPs) as scaffolding for biocatalysis. We genetically fuse TRAP domains and program them to selectively and orthogonally recognize peptide-tags fused to enzymes, which upon binding form spatially organized metabolomes. In addition, the scaffold encodes binding sites to selectively and reversibly sequester reaction intermediates like cofactors via electrostatic interactions, increasing their local concentration and, consequently, the catalytic efficiency. This concept is demonstrated for the biosynthesis of amino acids and amines using up to three enzymes. Scaffolded multi-enzyme systems present up to 5-fold higher specific productivity than the non-scaffolded ones. In-depth analysis suggests that channeling of NADH cofactor between the assembled enzymes enhances the overall cascade throughput and the product yield. Moreover, we immobilize this biomolecular scaffold on solid supports, creating reusable heterogeneous multi-functional biocatalysts for consecutive operational batch cycles. Our results demonstrate the potential of TRAP-scaffolding systems as spatial-organizing tools to increase the efficiency of cell-free biosynthetic pathways.
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.