Evidence map›Paper›PMID 24849696›Full record

ArticleChembiochem : a European journal of chemical biology2014

Improving the stability and catalyst lifetime of the halogenase RebH by directed evolution.

Catherine B Poor, Mary C Andorfer, Jared C Lewis

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

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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

3 authors.

Catherine B PoorDepartment of Chemistry, University of Chicago, 5735 S. Ellis Ave., Chicago, IL 60637 (USA).
Mary C Andorfer
Jared C Lewis

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Transition Metal Catalysis and Metabolic Engineering using Artificial MetalloenzyR00GM087551 · NIGMS · UNIVERSITY OF CHICAGO · PI LEWIS, JARED C · 2011 to 2013
$722k
NIGMS NIH HHS 5R00GM087551-03NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R00 GM087551
6 · The paper itself

Abstract

We previously reported that the halogenase RebH catalyzes selective halogenation of several heterocycles and carbocycles, but product yields were limited by enzyme instability. Here, we use directed evolution to engineer an RebH variant, 3-LR, with a Topt over 5 °C higher than that of wild-type, and 3-LSR, with a Tm 18 °C higher than that of wild-type. These enzymes provided significantly improved conversion (up to fourfold) for halogenation of tryptophan and several non-natural substrates. This initial evolution of RebH not only provides improved enzymes for immediate synthetic applications, but also establishes a robust protocol for further halogenase evolution.

Indexed as

BiocatalysisDirected Molecular EvolutionEnzyme StabilityModels, MolecularMolecular StructureOxidoreductasesProtein EngineeringOxidoreductasesbiocatalysisdirected evolutionhalogenasesRebHthermostability

Identifiers

PMID24849696
PMCPMC4124618

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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.