ArticleJournal of the American Chemical Society2013
Influence of active site location on catalytic activity in de novo-designed zinc metalloenzymes.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
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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
36 citing papers in PubMed.
- Design of a protein scaffold with a selective, Bi-containing heterodinuclear metal coordination motif.Journal of inorganic biochemistry · 2026Article
- 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
- Molecularly Imprinted Nanozymes for Selective Hydrolysis of Aromatic Carbonates Under Mild Conditions.Nanomaterials (Basel, Switzerland) · 2025Article
- Understanding Structural Isomerism in Organoiridium Picolinamidate Complexes and its Consequences on Reactivity and Biological Properties.Inorganic chemistry frontiers · 2024Article
- Co(II) Substitution Enhances the Esterase Activity of a de Novo Designed Zn(II) Carbonic Anhydrase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Article
- Carbonic anhydrase mimics with rationally designed active sites for fine-tuned catalytic activity and selectivity in ester hydrolysis.Catalysis science & technology · 2023Article
- Artificial Esterase for Cooperative Catalysis of Ester Hydrolysis at pH 7.Materials today. Chemistry · 2023Article
- Inside-Out Design of Zinc-Binding Proteins with Non-Native Backbones.Biochemistry · 2023Article
- Imprinted Polymeric Nanoparticles as Artificial Enzymes for Ester Hydrolysis at Room Temperature and pH 7.Chem catalysis · 2022Article
- Catalysis and Electron Transfer inChemical reviews · 2022Review
- De novo metalloprotein design.Nature reviews. Chemistry · 2022Article
- Biocatalysts Based on Peptide and Peptide Conjugate Nanostructures.Biomacromolecules · 2021Review
- Selective Hydrolysis of Aryl Esters under Acidic and Neutral Conditions by a Synthetic Aspartic Protease Mimic.ACS catalysis · 2021Article
- Catalysis and Electron Transfer in De Novo Designed Helical Scaffolds.Angewandte Chemie (International ed. in English) · 2020Review
- Heteromeric three-stranded coiled coils designed using a Pb(II)(Cys)Nature chemistry · 2020Article
- Review
- Engineering the hCRBPII Domain-Swapped Dimer into a New Class of Protein Switches.Journal of the American Chemical Society · 2019Article
- Selective coordination of three transition metal ions within a coiled-coil peptide scaffold.Chemical science · 2019Article
- Catalytic peptide assemblies.Chemical Society reviews · 2018Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
While metalloprotein design has now yielded a number of successful metal-bound and even catalytically active constructs, the question of where to put a metal site along a linear, repetitive sequence has not been thoroughly addressed. Often several possibilities in a given sequence may exist that would appear equivalent but may in fact differ for metal affinity, substrate access, or protein dynamics. We present a systematic variation of active site location for a hydrolytically active ZnHis3O site contained within a de novo-designed three-stranded coiled coil. We find that the maximal rate, substrate access, and metal-binding affinity are dependent on the selected position, while catalytic efficiency for p-nitrophenyl acetate hydrolysis can be retained regardless of the location of the active site. This achievement demonstrates how efficient, tailor-made enzymes which control rate, pKa, substrate and solvent access (and selectivity), and metal-binding affinity may be realized. These findings may be applied to the more advanced de novo design of constructs containing secondary interactions, such as hydrogen-bonding channels. We are now confident that changes to location for accommodating such channels can be achieved without location-dependent loss of catalytic efficiency. These findings bring us closer to our ultimate goal of incorporating the secondary interactions we believe will be necessary in order to improve both active site properties and the catalytic efficiency to be competitive with the native enzyme, carbonic anhydrase.
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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.