ArticleOrganic & biomolecular chemistry2013
The effect of the hydrophobic environment on the retro-aldol reaction: comparison to a computationally-designed enzyme.
Article in Organic & biomolecular chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Stimuli-Responsive Silsesquioxane Nanozymes for Organocatalysis in Water and Prodrug Activation in Cells.Angewandte Chemie (International ed. in English) · 2026Article
- Co-Assemblies Regulate the Catalytic Activity of Peptide Fibrils.Angewandte Chemie (International ed. in English) · 2026Article
- Article
- Design of an allosterically regulated retroaldolase.Protein science : a publication of the Protein Society · 2015Article
- Keep on moving: discovering and perturbing the conformational dynamics of enzymes.Accounts of chemical research · 2015Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Recent work on a computationally-designed retroaldolase RA-61 suggested that most of the rate-acceleration brought about by this enzyme was due to non-specific interactions with the aromatic substrate. To provide a benchmark for the role of non-specific interactions in this system, we measured the second-order rate constant for the amine-catalysed retro-aldol reaction of methodol in the presence of non-specific hydrophobic pockets such as micelles. We found that a simple micellar system, that consists of a positively-charged surfactant and a long-chain amine, can accelerate the retro-aldol reaction of methodol by 9500-fold. This effect rivals the 10(5)-fold rate acceleration of RA-61. Similar results were obtained with BSA used as the catalyst, implying that the retro-aldol reaction of methodol can be greatly accelerated by non-specific hydrophobic pockets that contain an amino group.
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