ArticleNature catalysis2019
Non-proteinaceous hydrolase comprised of a phenylalanine metallo-supramolecular amyloid-like structure.
Article in Nature catalysis, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
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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
47 citing papers in PubMed, 216 citations in OpenAlex.
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- Metal-dependent and metal-free mechanisms of peptide condensate catalysts.Nature communications · 2026Article
- Catalytic Amyloids: Turning Fibrils Into Biocatalysts.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Structure-activity relationships in catalytic amyloids.Journal of inorganic biochemistry · 2026Article
- Regulating Promiscuous Catalysis via Substrate-Induced Transient Assembly.Angewandte Chemie (International ed. in English) · 2026Article
- Multienzyme (3-in-1)-Mimicking a Single Nucleobase-Derived Bionanozyme for Versatile Environmental and Biomedical Applications.Advanced healthcare materials · 2025Article
- Coordination Geometry Tuning in a Single-Atom Nanozyme to Mimic Metalloenzymes with Nonplanar Active Site.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Condenzymes: Biomolecular condensates with inherent catalytic activities.bioRxiv : the preprint server for biology · 2025Article
- Amylum forms typical self-assembled amyloid fibrils.Science advances · 2024Article
- Site-selective peptide bond hydrolysis and ligation in water by short peptide-based assemblies.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Metal-ligand dual-site single-atom nanozyme mimicking urate oxidase with high substrates specificity.Nature communications · 2024Article
- 1-Naphthylacetic acid appended amino acids-based hydrogels: probing of the supramolecular catalysis of ester hydrolysis reaction.Nanoscale advances · 2024Article
- Emergence of a short peptide based reductase via activation of the model hydride rich cofactor.Nature communications · 2024Article
- Stopped-flow measurement of COMethods in enzymology · 2024Article
- Article
- Supramolecular peptide nanotubes as artificial enzymes for catalysing ester hydrolysis.Polymer chemistry · 2023Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Enzymatic activity is crucial for various technological applications, yet the complex structures and limited stability of enzymes often hinder their use. Hence, de novo design of robust biocatalysts that are much simpler than their natural counterparts and possess enhanced catalytic activity has long been a goal in biotechnology. Here, we present evidence for the ability of a single amino acid to self-assemble into a potent and stable catalytic structural entity. Spontaneously, phenylalanine (F) molecules coordinate with zinc ions to form a robust, layered, supramolecular amyloid-like ordered architecture (F-Zn(ii)) and exhibit remarkable carbonic anhydrase-like catalytic activity. Notably, amongst the reported artificial biomolecular hydrolases, F-Zn(ii) displays the lowest molecular mass and highest catalytic efficiency, in addition to reusability, thermal stability, substrate specificity, stereoselectivity and rapid catalytic CO
Identifiers
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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.