Literature DB >> 28795696

Inducing high activity of a thermophilic enzyme at ambient temperatures by directed evolution.

Guangyue Li1, Miguel A Maria-Solano2, Adrian Romero-Rivera2, Sílvia Osuna2, Manfred T Reetz1.   

Abstract

The long-standing problem of achieving high activity of a thermophilic enzyme at low temperatures and short reaction times with little tradeoff in thermostability has been solved by directed evolution, an alcohol dehydrogenase found in hot springs serving as the catalyst in enantioselective ketone reductions.

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Year:  2017        PMID: 28795696     DOI: 10.1039/c7cc05377k

Source DB:  PubMed          Journal:  Chem Commun (Camb)        ISSN: 1359-7345            Impact factor:   6.222


  4 in total

Review 1.  Protein folding and surface interaction phase diagrams in vitro and in cells.

Authors:  Martin Gruebele
Journal:  FEBS Lett       Date:  2021-03-27       Impact factor: 4.124

Review 2.  Role of conformational dynamics in the evolution of novel enzyme function.

Authors:  Miguel A Maria-Solano; Eila Serrano-Hervás; Adrian Romero-Rivera; Javier Iglesias-Fernández; Sílvia Osuna
Journal:  Chem Commun (Camb)       Date:  2018-06-19       Impact factor: 6.222

3.  Establishment of mesophilic-like catalytic properties in a thermophilic enzyme without affecting its thermal stability.

Authors:  Satoshi Akanuma; Mizumo Bessho; Hikono Kimura; Ryutaro Furukawa; Shin-Ichi Yokobori; Akihiko Yamagishi
Journal:  Sci Rep       Date:  2019-06-27       Impact factor: 4.379

4.  "NAD-display": Ultrahigh-Throughput in Vitro Screening of NAD(H) Dehydrogenases Using Bead Display and Flow Cytometry.

Authors:  Laurens Lindenburg; Florian Hollfelder
Journal:  Angew Chem Int Ed Engl       Date:  2021-03-08       Impact factor: 15.336

  4 in total

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