ArticleNature chemistry2011
Hydrolytic catalysis and structural stabilization in a designed metalloprotein.
Article in Nature chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 142 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
142 citing papers in PubMed.
- Modulating thermal folded stability and catalytic activity of aRSC advances · 2026Article
- Conserved catalytic motifs encode enzyme-like supramolecular peptide assemblies.Research square · 2026Article
- Biomolecular condensates can function as inherent catalysts.Molecular cell · 2026Article
- Design of a site selective heterochromic bimetallic lanthanide coiled coil with nanometre-scale control.Chemical science · 2026Article
- Zero-shot design of abioRxiv : the preprint server for biology · 2026Article
- Probing anion recognition in a cobalt(II) de novo designed metalloprotein.Journal of inorganic biochemistry · 2026Article
- A bis-macrocylic peptide ligand mimicking the β-sandwich active site of multicopper oxidases.Dalton transactions (Cambridge, England : 2003) · 2026Article
- Structure-activity relationships in catalytic amyloids.Journal of inorganic biochemistry · 2026Article
- Computational design of metallohydrolases.Nature · 2026Article
- Design of a protein scaffold with a selective, Bi-containing heterodinuclear metal coordination motif.Journal of inorganic biochemistry · 2026Article
- Dual-function hemoglobin-encapsulating ZIF-8 nanoparticles: Oxygen transport capability and carbonic anhydrase-like activity.Materials today. Bio · 2025Article
- Article
- Assembled peptoid crystalline nanomaterials as carbonic anhydrase mimics for promoted hydration and sequestration of CONature communications · 2025Article
- A cytokine-based designer enzyme with an abiological multinuclear metal center exhibits intrinsic and extrinsic catalysis.Nature communications · 2025Article
- Recent advances in de novo designed metallopeptides as tailored enzyme mimics.Current opinion in chemical biology · 2025Review
- Condenzymes: Biomolecular condensates with inherent catalytic activities.bioRxiv : the preprint server for biology · 2025Article
- Artificial metalloenzyme assembly in cellular compartments for enhanced catalysis.Nature chemical biology · 2025Article
- Computational design of serine hydrolases.Science (New York, N.Y.) · 2025Article
- A semisynthetic, multicofactor artificial metalloenzyme retains independent site activity.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Article
- Molecularly Imprinted Nanozymes for Selective Hydrolysis of Aromatic Carbonates Under Mild Conditions.Nanomaterials (Basel, Switzerland) · 2025Article
82 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Metal ions are an important part of many natural proteins, providing structural, catalytic and electron transfer functions. Reproducing these functions in a designed protein is the ultimate challenge to our understanding of them. Here, we present an artificial metallohydrolase, which has been shown by X-ray crystallography to contain two different metal ions-a Zn(II) ion, which is important for catalytic activity, and a Hg(II) ion, which provides structural stability. This metallohydrolase displays catalytic activity that compares well with several characteristic reactions of natural enzymes. It catalyses p-nitrophenyl acetate (pNPA) hydrolysis with an efficiency only ~100-fold less than that of human carbonic anhydrase (CA)II and at least 550-fold better than comparable synthetic complexes. Similarly, CO(2) hydration occurs with an efficiency within ~500-fold of CAII. Although histidine residues in the absence of Zn(II) exhibit pNPA hydrolysis, miniscule apopeptide activity is observed for CO(2) hydration. The kinetic and structural analysis of this first de novo designed hydrolytic metalloenzyme reveals necessary design features for future metalloenzymes containing one or more metals.
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.