Two separate peptides in Escherichia coli methionyl-tRNA synthetase form the anticodon binding site for methionine tRNA

Biochemistry ◽  
1993 ◽  
Vol 32 (39) ◽  
pp. 10506-10511 ◽  
Author(s):  
Hae Yeong Kim ◽  
Heike Pelka ◽  
Simone Brunie ◽  
LaDonne H. Schulman
2020 ◽  
Vol 209 (2) ◽  
pp. 107435 ◽  
Author(s):  
Giuliano Nigro ◽  
Sophie Bourcier ◽  
Christine Lazennec-Schurdevin ◽  
Emmanuelle Schmitt ◽  
Philippe Marlière ◽  
...  

2005 ◽  
Vol 127 (3) ◽  
pp. 449-457 ◽  
Author(s):  
David G. BARKER ◽  
Jean-Pierre EBEL ◽  
Ross JAKES ◽  
Chris J. BRUTON

1975 ◽  
Vol 21 (6) ◽  
pp. 754-758 ◽  
Author(s):  
John B. Armstrong ◽  
John A. Fairfield

Six methionine auxotrophs were isolated from an E. coli K-12 strain which required up to 100 times as much methionine for growth as a conventional auxotroph. In these mutants, the methionyl-tRNA synthetase had an increased Km for methionine. The Km value for the mutants ranged from 0.48 to 1.63 mM, compared to 0.078 mM for the wild type. The Km (methionine) for S-adenosyl methionine synthetase was not altered.


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