Crystallization of the Malonyl Coenzyme A-Acyl Carrier Protein Transacylase from Escherichia coli

1994 ◽  
Vol 242 (1) ◽  
pp. 99-102 ◽  
Author(s):  
Laurence Serre ◽  
Lora Swenson ◽  
Ruth Green ◽  
Yunju Wei ◽  
Ira I.G.S. Verwoert ◽  
...  
1974 ◽  
Vol 249 (23) ◽  
pp. 7468-7475
Author(s):  
Mark E. Harder ◽  
Ruth C. Ladenson ◽  
Steven D. Schimmel ◽  
David F. Silbert

1982 ◽  
Vol 152 (3) ◽  
pp. 1298-1300
Author(s):  
C O Rock

Three soluble proteins in Escherichia coli specifically from mixed disulfides with either acyl carrier protein or coenzyme A. Coenzyme A was attached to one of these proteins, and the amount bound depended on the cellular coenzyme A concentration. The other two proteins were mixed disulfides between acyl carrier protein and each of the two 3-ketoacyl-acyl carrier protein synthases.


2004 ◽  
Vol 70 (7) ◽  
pp. 3807-3813 ◽  
Author(s):  
Zhong Zheng ◽  
Qiang Gong ◽  
Tao Liu ◽  
Ying Deng ◽  
Jin-Chun Chen ◽  
...  

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.


1973 ◽  
Vol 248 (12) ◽  
pp. 4461-4466
Author(s):  
Gary L. Powell ◽  
Michael Bauza ◽  
Allan R. Larrabee

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