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Applied and Environmental Microbiology, July 2004, p. 3807-3813, Vol. 70, No. 7
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.7.3807-3813.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

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

Zhong Zheng,1 Qiang Gong,1 Tao Liu,2 Ying Deng,3 Jin-Chun Chen,1 and Guo-Qiang Chen1*

MOE Laboratory of Protein Science, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084,1 School of Life Science, Shandong University, Jinan 250100,2 Multidisciplinary Research Center, Shantou University, Guangdong 515063, China3

Received 13 January 2004/ Accepted 27 February 2004

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.

* Corresponding author. Mailing address: MOE Laboratory of Protein Science, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China. Phone: 86-10-62783844. Fax: 86-10-62788784. E-mail: chengq{at}mail.tsinghua.edu.cn.

Applied and Environmental Microbiology, July 2004, p. 3807-3813, Vol. 70, No. 7
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.7.3807-3813.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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