Thioesterase II of Escherichia coli plays an important role in 3-hydroxydecanoic acid production.
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.
Zheng
Zhong
Z
MOE Laboratory of Protein Science, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China.
Gong
Qiang
Q
Liu
Tao
T
Deng
Ying
Y
Chen
Jin-Chun
JC
Chen
Guo-Qiang
GQ
D003652:Decanoic Acids / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D064429:Fatty Acid Synthases / Q000502:physiology*; D011994:Recombinant Proteins / Q000096:biosynthesis; D013869:Thiolester Hydrolases / Q000502:physiology*
D003652:Decanoic Acids; D011994:Recombinant Proteins; D064429:Fatty Acid Synthases; D013869:Thiolester Hydrolases; C022738:thioesterase II; C017552:myrmicacin