scholarly journals Metabolic engineering for the production of shikimic acid in an evolved Escherichia coli strain lacking the phosphoenolpyruvate: carbohydrate phosphotransferase system

2010 ◽  
Vol 9 (1) ◽  
pp. 21 ◽  
Author(s):  
Adelfo Escalante ◽  
Rocío Calderón ◽  
Araceli Valdivia ◽  
Ramón de Anda ◽  
Georgina Hernández ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Metabolic Engineering ◽  
Shikimic Acid ◽  
Coli Strain ◽  
Phosphotransferase System

Designing an Escherichia coli Strain for Phenylalanine Overproduction by Metabolic Engineering

2017 ◽  
Vol 59 (4-5) ◽  
pp. 168-178 ◽  
Author(s):  
Neetu Tyagi ◽  
Deepti Saini ◽  
Richa Guleria ◽  
Krishna Jyoti Mukherjee
Keyword(s):  
Escherichia Coli ◽  
Metabolic Engineering ◽  
Coli Strain

Metabolic engineering of a robust Escherichia coli strain with a dual protection system

2019 ◽  
Vol 116 (12) ◽  
pp. 3333-3348 ◽  
Author(s):  
Xiao‐Yang Ou ◽  
Xiao‐Ling Wu ◽  
Fei Peng ◽  
Ying‐Jie Zeng ◽  
Hui‐Xian Li ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Metabolic Engineering ◽  
Coli Strain ◽  
Protection System ◽  
Dual Protection

Isolation and characterization of catabolite repression-resistant mutants of Escherichia coli

1977 ◽  
Vol 23 (10) ◽  
pp. 1384-1393 ◽  
Author(s):  
Glen D. Armstrong ◽  
Hiroshi Yamazaki
Keyword(s):  
Escherichia Coli ◽  
Catabolite Repression ◽  
Coli Strain ◽  
Wild Type ◽  
Phosphotransferase System ◽  
E Coli ◽  
Isolation And Characterization ◽  
In The Wild ◽  
Resistant Mutants

A method has been developed for the isolation of Escherichia coli mutants which are resistant to catabolite repression. The method is based on the fact that a mixture of glucose and gluconate inhibits the development of chemotactic motility in the wild type, but not in the mutants. A motile E. coli strain was mutagenized and grown in glucose and gluconate. Mutants which were able to swim into a tube containing a chemotactic attractant (aspartic acid) were isolated. Most of these mutants were able to produce β-galactosidase in the presence of glucose and gluconate and were normal in their ability to degrade adenosine 3′,5′-cyclic monophosphate. Some of these mutants were defective in the glucose phosphotransferase system.

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