Evidence map›Paper›PMID 33687787›Full record

ArticleAngewandte Chemie (International ed. in English)2021

Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance.

Haiyang Cui, Lobna Eltoukhy, Lingling Zhang, Ulrich Markel, Karl-Erich Jaeger, Mehdi D Davari, Ulrich Schwaneberg

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed, 1 pooled it
–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

19 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  12. Rational design of enzyme activity and enantioselectivity.Frontiers in bioengineering and biotechnology · 2023
    Review
  13. A Plurizyme with Transaminase and Hydrolase Activity Catalyzes Cascade Reactions.Angewandte Chemie (International ed. in English) · 2022
    Article
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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

7 authors.

Haiyang CuiInstitute of Biotechnology, RWTH Aachen University, Worringer Weg 3, 52074, Aachen, Germany.ORCID 0000-0001-8360-0447
Lobna EltoukhyInstitute of Biotechnology, RWTH Aachen University, Worringer Weg 3, 52074, Aachen, Germany.
Lingling ZhangInstitute of Biotechnology, RWTH Aachen University, Worringer Weg 3, 52074, Aachen, Germany.ORCID 0000-0002-3384-2576
Ulrich MarkelInstitute of Biotechnology, RWTH Aachen University, Worringer Weg 3, 52074, Aachen, Germany.ORCID 0000-0002-5655-5342
Karl-Erich JaegerInstitute of Molecular Enzyme Technology, Heinrich Heine University Düsseldorf, Wilhelm Johnen Strasse, 52426, Jülich, Germany.ORCID 0000-0002-6036-0708
Mehdi D DavariInstitute of Biotechnology, RWTH Aachen University, Worringer Weg 3, 52074, Aachen, Germany.ORCID 0000-0003-0089-7156
Ulrich SchwanebergInstitute of Biotechnology, RWTH Aachen University, Worringer Weg 3, 52074, Aachen, Germany.ORCID 0000-0003-4026-701X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biocatalysis for the synthesis of fine chemicals is highly attractive but usually requires organic (co-)solvents (OSs). However, native enzymes often have low activity and resistance in OSs and at elevated temperatures. Herein, we report a smart salt bridge design strategy for simultaneously improving OS resistance and thermostability of the model enzyme, Bacillus subtilits Lipase A (BSLA). We combined comprehensive experimental studies of 3450 BSLA variants and molecular dynamics simulations of 36 systems. Iterative recombination of four beneficial substitutions yielded superior resistant variants with up to 7.6-fold (D64K/D144K) improved resistance toward three OSs while exhibiting significant thermostability (thermal resistance up to 137-fold, and half-life up to 3.3-fold). Molecular dynamics simulations revealed that locally refined flexibility and strengthened hydration jointly govern the highly increased resistance in OSs and at 50-100 °C. The salt bridge redesign provides protein engineers with a powerful and likely general approach to design OSs- and/or thermal-resistant lipases and other α/β-hydrolases.

Indexed as

Bacillus subtilisBiocatalysisEnzyme StabilityLipaseMolecular Dynamics SimulationOrganic ChemicalsProtein ConformationSaltsSolventsTemperatureLipaseOrganic ChemicalsSaltsSolventsbacillus subtilits lipase A (BSLA)directed evolutionorganic solvent resistancerational designsalt bridge

Identifiers

PMID33687787
PMCPMC8252522

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.