Literature DB >> 25415647

A thermostable transketolase evolved for aliphatic aldehyde acceptors.

Dong Yi1, Thangavelu Saravanan, Titu Devamani, Franck Charmantray, Laurence Hecquet, Wolf-Dieter Fessner.   

Abstract

Directed evolution of the thermostable transketolase from Geobacillus stearothermophilus based on a pH-based colorimetric screening of smart libraries yielded several mutants with up to 16-fold higher activity for aliphatic aldehydes and high enantioselectivity (>95% ee) in the asymmetric carboligation step.

Entities:  

Mesh：

Substances：

Year:  2014        PMID： 25415647     DOI： 10.1039/c4cc08436e

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


  4 in total

1.  Droplet millifluidics for kinetic study of transketolase.

Authors:  A Pinsolle; F Charmantray; L Hecquet; F Sarrazin
Journal:  Biomicrofluidics       Date:  2016-11-10       Impact factor: 2.800

2.  Two strategies to engineer flexible loops for improved enzyme thermostability.

Authors:  Haoran Yu; Yihan Yan; Cheng Zhang; Paul A Dalby
Journal:  Sci Rep       Date:  2017-02-01       Impact factor: 4.379

3.  Separating Thermodynamics from Kinetics-A New Understanding of the Transketolase Reaction.

Authors:  Stefan R Marsden; Lorina Gjonaj; Stephen J Eustace; Ulf Hanefeld
Journal:  ChemCatChem       Date:  2017-04-13       Impact factor: 5.686

4.  Assessing the Thiamine Diphosphate Dependent Pyruvate Dehydrogenase E1 Subunit for Carboligation Reactions with Aliphatic Ketoacids.

Authors:  Stefan R Marsden; Duncan G G McMillan; Ulf Hanefeld
Journal:  Int J Mol Sci       Date:  2020-11-16       Impact factor: 5.923
  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.