Evidence map›Paper›PMID 27162418›Full record

ArticleJournal of physical organic chemistry2016

Kemp Elimination in Cationic Micelles: Designed Enzyme-Like Rates Achieved through the Addition of Long-Chain Bases.

Enis Sanchez, Steven Lu, Carson Reed, Joshua Schmidt, Marcello Forconi

Abstract read
In one paragraph

Article in Journal of physical organic chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Review
  2. Integrative Role of Albumin: Evolutionary, Biochemical and Pathophysiological Aspects.Journal of evolutionary biochemistry and physiology · 2021
    Article
  3. Enhancing aChemical science · 2020
    Article
  4. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Enis SanchezDepartment of Chemistry and Biochemistry, College of Charleston, 202 Calhoun St, Charleston, SC 29424, U.S.A.
Steven LuAcademic Magnet High School, 5109 W Enterprise St, North Charleston, SC 29405. U.S.A.
Carson ReedDepartment of Chemistry and Biochemistry, College of Charleston, 202 Calhoun St, Charleston, SC 29424, U.S.A.
Joshua SchmidtDepartment of Chemistry and Biochemistry, College of Charleston, 202 Calhoun St, Charleston, SC 29424, U.S.A.
Marcello ForconiDepartment of Chemistry and Biochemistry, College of Charleston, 202 Calhoun St, Charleston, SC 29424, U.S.A.

Funding

South Carolina IDeA Networks of Biomedical Research (SC INBRE V)P20GM103499 · NIGMS · UNIVERSITY OF SOUTH CAROLINA AT COLUMBIA · PI EDIE C GOLDSMITH · 2012 to 2026
$61.0M
NIGMS NIH HHS P20 GM103499
6 · The paper itself

Abstract

The Kemp elimination is prototypical reaction used to study proton abstraction from carbon. Several hydrophobic systems are known to accelerate this reaction, including two classes of computationally-designed enzymes. However, it is unclear whether these computationally-designed enzymes establish specific interactions with their substrates, as natural enzymes do, or if most of the rate acceleration is due to the hydrophobicity of the substrate. We used a simple system composed of cationic micelles and a long chain base (such as lauryl phosphate or lauric acid) to measure the rate acceleration for the Kemp elimination. Remarkably, we found that this simple system can accelerate the reaction by 4 orders of magnitude, approaching the rates of more complex designed systems. Use of different substrates suggests that the reaction takes place at the interface between the micellar head and water (the Stern layer) with the long-chain base embedded in the micelle and the substrate in the aqueous solution. Thus, we suggest that significant rate accelerations can be achieved regardless of the precise positioning of substrates. Because natural enzymes use specific interactions to position their substrates, we propose that acceleration of the Kemp elimination is not a suitable benchmark for the success of the design process, and we suggest that more complex reactions should be used.

Indexed as

catalysisenzyme designhydrophobic interactionsKemp eliminationmicelles

Identifiers

PMID27162418
PMCPMC4859443

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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.