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Inside Back Cover: Second‐Generation Engineering of a Thermostable Transketolase (TK Gst ) for Aliphatic Aldehyde Acceptors with Either Improved or Reversed Stereoselectivity (ChemBioChem 5/2017)
Author(s) -
Zhou Chaoqiang,
Saravanan Thangavelu,
Lorillière Marion,
Wei Dongzhi,
Charmantray Franck,
Hecquet Laurence,
Fessner WolfDieter,
Yi Dong
Publication year - 2017
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201700044
Subject(s) - transketolase , saturated mutagenesis , aldehyde , stereoselectivity , chemistry , mutagenesis , stereochemistry , biocatalysis , geobacillus stearothermophilus , lithium (medication) , biochemistry , mutation , biology , enzyme , thermophile , reaction mechanism , gene , catalysis , mutant , endocrinology
The inside back cover picture shows two positive variants of thermostable transketolase from Geobacillus stearothermophilus (TK Gst ) obtained by saturation mutagenesis at the 191, 435, and 470 positions “discussing” their roughly fivefold improved activity towards non‐α‐hydroxy aldehyde acceptors, as well as the inversed stereoconfiguration of their 4‐deoxyketose products, which have more than 70 % ee starting from lithium hydroxypyruvate as donor and non‐α‐hydroxy aldehydes as acceptors. More information can be found in the communication by D. Yi et al. on page 455 in Issue 5, 2017 (DOI: 10.1002/cbic.201600609).