scholarly journals Regulation of fatty acid synthesis during the cessation of phospholipid biosynthesis in Escherichia coli.

1977 ◽  
Vol 132 (2) ◽  
pp. 526-531 ◽  
Author(s):  
W D Nunn ◽  
D L Kelly ◽  
M Y Stumfall
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Acid Synthesis ◽  
Phospholipid Biosynthesis

scholarly journals Boosting the free fatty acid synthesis of Escherichia coli by expression of a cytosolic Acinetobacter baylyi thioesterase

2012 ◽  
Vol 5 (1) ◽  
pp. 76 ◽  
Author(s):  
Yanning Zheng ◽  
Lingling Li ◽  
Qiang Liu ◽  
Jianming Yang ◽  
Yujin Cao ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Free Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Acid Synthesis ◽  
Acinetobacter Baylyi

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 ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Acid Synthesis

scholarly journals Alternate fatty acid synthesis initiation in Escherichia coli

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Sarah G. Whaley ◽  
Charles O. Rock
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Acid Synthesis

scholarly journals Expression in Escherichia coli, purification and characterization of two mammalian thioesterases involved in fatty acid synthesis

1991 ◽  
Vol 273 (3) ◽  
pp. 787-790 ◽  
Author(s):  
J Naggert ◽  
A Witkowski ◽  
B Wessa ◽  
S Smith
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Fatty Acid Synthase ◽  
De Novo ◽  
Acid Synthesis ◽  
Temperature Sensitive ◽  
Lambda Repressor ◽  
Thioesterase Ii ◽  
Chain Lengths

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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