Redesigning the Substrate Specificity of an Enzyme by Cumulative Effects of the Mutations of Non-active Site Residues

Directed evolution was used to change the substrate specificity of aspartate aminotransferase. A mutant enzyme with 17 amino acid substitutions was generated that shows a 2.1 x 10(6)-fold increase in the catalytic efficiency (kcat/Km) for a non-native substrate, valine. The absorption spectrum of th...

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Main Authors: Shinya Oue, Akihiro Okamoto, T. Yano, Hiroyuki Kagamiyama
格式: Artigo
语言:英语
出版: 1999
在线阅读:https://doi.org/10.1074/jbc.274.4.2344
http://www.jbc.org/article/S0021925819881838/pdf
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