Evidence map›Paper›PMID 26527505›Full record

ArticleACS catalysis2015

Expanding the Catalytic Triad in Epoxide Hydrolases and Related Enzymes.

Beat A Amrein, Paul Bauer, Fernanda Duarte, Åsa Janfalk Carlsson, Agata Naworyta, Sherry L Mowbray, Mikael Widersten, Shina C L Kamerlin

Open access · bronzeAbstract read
In one paragraph

Article in ACS catalysis, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.5field-weighted citation impact, top 7% of its field
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

21 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  7. The Mechanism of Biochemical NO-Sensing: Insights from Computational Chemistry.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022
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  12. ExploringBiomolecules · 2018
    Article
  13. Review
  14. Article
  15. Article
  16. IUCrJ · 2017
    Article
  17. Computational tools for the evaluation of laboratory-engineered biocatalysts.Chemical communications (Cambridge, England) · 2016
    Review
  18. Article
  19. Article
  20. 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

8 authors at 2 institutions in 1 country.

Beat A AmreinScience for Life Laboratory, Department of Cell and Molecular Biology, Uppsala University , BMC Box 596, SE-751 24 Uppsala, Sweden.
Paul BauerScience for Life Laboratory, Department of Cell and Molecular Biology, Uppsala University , BMC Box 596, SE-751 24 Uppsala, Sweden.
Fernanda DuarteScience for Life Laboratory, Department of Cell and Molecular Biology, Uppsala University , BMC Box 596, SE-751 24 Uppsala, Sweden.
Åsa Janfalk CarlssonDepartment of Chemistry-BMC, Uppsala University , BMC Box 576, SE-751 23 Uppsala, Sweden.
Agata NaworytaScience for Life Laboratory, Department of Cell and Molecular Biology, Uppsala University , BMC Box 596, SE-751 24 Uppsala, Sweden.
Sherry L MowbrayScience for Life Laboratory, Department of Cell and Molecular Biology, Uppsala University , BMC Box 596, SE-751 24 Uppsala, Sweden.
Mikael WiderstenDepartment of Chemistry-BMC, Uppsala University , BMC Box 576, SE-751 23 Uppsala, Sweden.
Shina C L KamerlinScience for Life Laboratory, Department of Cell and Molecular Biology, Uppsala University , BMC Box 596, SE-751 24 Uppsala, Sweden.
Uppsala University · SEScience for Life Laboratory · SE

Funding

European Research Council 306474
6 · The paper itself

Abstract

Potato epoxide hydrolase 1 exhibits rich enantio- and regioselectivity in the hydrolysis of a broad range of substrates. The enzyme can be engineered to increase the yield of optically pure products as a result of changes in both enantio- and regioselectivity. It is thus highly attractive in biocatalysis, particularly for the generation of enantiopure fine chemicals and pharmaceuticals. The present work aims to establish the principles underlying the activity and selectivity of the enzyme through a combined computational, structural, and kinetic study using the substrate

Indexed as

biocatalysisempirical valence bondenzyme selectivitypotato epoxide hydrolaseStEH1trans-stilbene oxideX-ray crystallography

Identifiers

PMID26527505
PMCPMC4613740
OpenAlexW1415362898

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.