Improved pinocembrin production in Escherichia coli by engineering fatty acid synthesis

2016 ◽  
Vol 43 (4) ◽  
pp. 557-566 ◽  
Author(s):  
Weijia Cao ◽  
Weichao Ma ◽  
Bowen Zhang ◽  
Xin Wang ◽  
Kequan Chen ◽  
...  
2012 ◽  
Vol 5 (1) ◽  
pp. 76 ◽  
Author(s):  
Yanning Zheng ◽  
Lingling Li ◽  
Qiang Liu ◽  
Jianming Yang ◽  
Yujin Cao ◽  
...  

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Sarah G. Whaley ◽  
Charles O. Rock

1991 ◽  
Vol 273 (3) ◽  
pp. 787-790 ◽  
Author(s):  
J Naggert ◽  
A Witkowski ◽  
B Wessa ◽  
S Smith

Thioesterase I, a constituent domain of the multifunctional fatty acid synthase, and thioesterase II, an independent monofunctional protein, catalyse the chain-terminating reaction in fatty acid synthesis de novo at long and medium chain lengths respectively. The enzymes have been cloned and expressed in Escherichia coli under the control of the temperature-sensitive lambda repressor. The recombinant proteins are full-length catalytically competent thioesterases with specificities indistinguishable from those of the natural enzymes.


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