ReviewCurrent opinion in structural biology2014
Catalytic efficiency of designed catalytic proteins.
Review in Current opinion in structural biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 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
42 citing papers in PubMed.
- Conserved catalytic motifs encode enzyme-like supramolecular peptide assemblies.Research square · 2026Article
- Catalytic Amyloids: Turning Fibrils Into Biocatalysts.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Article
- Article
- Highly efficient enzymes designed from scratch.Nature · 2025Article
- Confinement and Catalysis withinJournal of the American Chemical Society · 2025Article
- Stopped-flow measurement of COMethods in enzymology · 2024Article
- From random to rational: improving enzyme design through electric fields, second coordination sphere interactions, and conformational dynamics.Chemical science · 2023Review
- Fishing for Catalysis: Experimental Approaches to Narrowing Search Space in Directed Evolution of Enzymes.JACS Au · 2023Review
- Ensemble-function relationships to dissect mechanisms of enzyme catalysis.Science advances · 2022Article
- Assessing and enhancing foldability in designed proteins.Protein science : a publication of the Protein Society · 2022Article
- What Have We Learned from Design of Function in Large Proteins?Biodesign research · 2022Review
- A bound iron porphyrin is redox active in hybrid bacterial reaction centers modified to possess a four-helix bundle domain.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Article
- Enzyme modification using mutation site prediction method for enhancing the regioselectivity of substrate reaction sites.Scientific reports · 2021Article
- Biocatalysts Based on Peptide and Peptide Conjugate Nanostructures.Biomacromolecules · 2021Review
- Acyl Transfer Catalytic Activity in De Novo Designed Protein with N-Terminus of α-Helix As Oxyanion-Binding Site.Journal of the American Chemical Society · 2021Article
- Extension of an Atom-Atom Dispersion Function to Halogen Bonds and Its Use for Rational Design of Drugs and Biocatalysts.The journal of physical chemistry. A · 2021Article
- Primitive selection of the fittest emerging through functional synergy in nucleopeptide networks.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Catalytic Principles from Natural Enzymes and Translational Design Strategies for Synthetic Catalysts.ACS central science · 2021Review
- MinimalistACS catalysis · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
The de novo design of catalysts that mimic the affinity and specificity of natural enzymes remains one of the Holy Grails of chemistry. Despite decades of concerted effort we are still unable to design catalysts as efficient as enzymes. Here we critically evaluate approaches to (re)design of novel catalytic function in proteins using two test cases: Kemp elimination and ester hydrolysis. We show that the degree of success thus far has been modest when the rate enhancements seen for the designed proteins are compared with the rate enhancements by small molecule catalysts in solvents with properties similar to the active site. Nevertheless, there are reasons for optimism: the design methods are ever improving and the resulting catalyst can be efficiently improved using directed evolution.
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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.