Expression and characterization of a structural and functional domain of the mannitol-specific transport protein involved in the coupling of mannitol transport and phosphorylation in the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli

Biochemistry ◽  
1993 ◽  
Vol 32 (37) ◽  
pp. 9553-9562 ◽  
Author(s):  
G. T. Robillard ◽  
H. Boer ◽  
R. P. van Weeghel ◽  
G. Wolters ◽  
A. Dijkstra
Keyword(s):  
Escherichia Coli ◽  
Transport Protein ◽  
Functional Domain ◽  
Phosphotransferase System ◽  
Specific Transport

Characterization of sugar mixtures utilization by an Escherichia coli mutant devoid of the phosphotransferase system

2001 ◽  
Vol 57 (1-2) ◽  
pp. 186-191 ◽  
Author(s):  
Hernández-Montalvo V. ◽  
Valle F. ◽  
Bolivar F. ◽  
Gosset G.
Keyword(s):  
Escherichia Coli ◽  
Phosphotransferase System ◽  
Coli Mutant ◽  
Sugar Mixtures

scholarly journals Characterization of MtfA, a Novel Regulatory Output Signal Protein of the Glucose-Phosphotransferase System in Escherichia coli K-12

2011 ◽  
Vol 194 (5) ◽  
pp. 1024-1035 ◽  
Author(s):  
A.-K. Gohler ◽  
A. Staab ◽  
E. Gabor ◽  
K. Homann ◽  
E. Klang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Output Signal ◽  
Phosphotransferase System ◽  
K 12

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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