scholarly journals The Effect of Amino Acid Analogues on Alkaline Phosphatase Formation in Escherichia coli K-12

1969 ◽  
Vol 244 (14) ◽  
pp. 3803-3809
Author(s):  
S Schlesinger ◽  
M J Schlesigner
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Amino Acid ◽  
Amino Acid Analogues ◽  
K 12

scholarly journals Glutamyl-γ-methyl ester acts as a methionine analogue inEscherichia coli: analogue resistant mutants map at themetJandmetKloci

1979 ◽  
Vol 33 (1) ◽  
pp. 49-55 ◽  
Author(s):  
Jan Kraus ◽  
Dieter Soll ◽  
K. Brooks Low
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Methyl Ester ◽  
Gene Order ◽  
Cross Resistance ◽  
Inescherichia Coli ◽  
Amino Acid Analogues ◽  
Resistant Mutants ◽  
K 12

SUMMARYEscherichia coliK-12 mutants resistant to glutamyl-γ-methyl ester were isolated. A mutation leading to resistance of up to 1·4 mg/ml of the methionine analogue maps at min 63 and is 13% cotransducible withserAindicating an alteration in themetKgene. Another mutation leading to resistance to 3 mg/ml of the analogue and cross-resistance to other amino acid analogues maps at min 87. This mutation, which has the phenotype of MetJ−, is shown to be situated between theglpKandmetBgenes and thus indicates a different gene order from the published one.

scholarly journals Point Mutations in Transmembrane Helices 2 and 3 of ExbB and TolQ Affect Their Activities in Escherichia coli K-12

2004 ◽  
Vol 186 (13) ◽  
pp. 4402-4406 ◽  
Author(s):  
Volkmar Braun ◽  
Christina Herrmann
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Transmembrane Helix ◽  
Point Mutations ◽  
Transmembrane Helices ◽  
The Third ◽  
Form Part ◽  
K 12

ABSTRACT Replacement of glutamate 176, the only charged amino acid in the third transmembrane helix of ExbB, with alanine (E176A) abolished ExbB activity in all determined ExbB-dependent functions of Escherichia coli. Combination of the mutations T148A in the second transmembrane helix and T181A in the third transmembrane helix, proposed to form part of a proton pathway through ExbB, also resulted in inactive ExbB. E176 and T148 are strictly conserved in ExbB and TolQ proteins, and T181 is almost strictly conserved in ExbB, TolQ, and MotA.

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