Thioesterase II of Escherichia coli Plays an Important Role in 3-Hydroxydecanoic Acid Production

Author:

Zheng Zhong1,Gong Qiang1,Liu Tao2,Deng Ying3,Chen Jin-Chun1,Chen Guo-Qiang1

Affiliation:

1. MOE Laboratory of Protein Science, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084

2. School of Life Science, Shandong University, Jinan 250100

3. Multidisciplinary Research Center, Shantou University, Guangdong 515063, China

Abstract

ABSTRACT 3-Hydroxydecanoic acid (3HD) was produced in Escherichia coli by mobilizing ( R )-3-hydroxydecanoyl-acyl carrier protein-coenzyme A transacylase (PhaG, encoded by the phaG gene). By employing an isogenic tesB (encoding thioesterase II)-negative knockout E. coli strain, CH01, it was found that the expressions of tesB and phaG can up-regulate each other. In addition, 3HD was synthesized from glucose or fructose by recombinant E. coli harboring phaG and tesB . This study supports the hypothesis that the physiological role of thioesterase II in E. coli is to prevent the abnormal accumulation of intracellular acyl-coenzyme A.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

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