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Updated: May 5, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
Molecular evolution of threonine dehydratase in bacteria
Xuefei Yu1, Ye Li, Xiaoyuan Wang
1State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, China ; Key Laboratory of Industrial Biotechnology of Ministry of Education, Jiangnan University, Wuxi, China.
Abstract:
Threonine dehydratase converts L-threonine to 2-ketobutyrate. Several threonine dehydratases exist in bacteria, but their origins and evolutionary pathway are unknown. Here we analyzed all the available threonine dehydratases in bacteria and proposed an evolutionary pathway leading to the genes encoding three different threonine dehydratases CTD, BTD1 and BTD2. The ancestral threonine dehydratase might contain only a catalytic domain, but one or two ACT-like subdomains were fused during the evolution, resulting BTD1 and BTD2, respectively. Horizontal gene transfer, gene fusion, gene duplication, and gene deletion may occur during the evolution of this enzyme. The results are important for understanding the functions of various threonine dehydratases found in bacteria.
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