Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase

Biochemistry ◽  
1993 ◽  
Vol 32 (34) ◽  
pp. 8758-8771 ◽  
Author(s):  
John J. Perona ◽  
Mark A. Rould ◽  
Thomas A. Steitz
Author(s):  
Alfredo Torres-Larios ◽  
Anne-Catherine Dock-Bregeon ◽  
Pascale Romby ◽  
Bernard Rees ◽  
Rajan Sankaranarayanan ◽  
...  

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.


1984 ◽  
Vol 81 (16) ◽  
pp. 5076-5080 ◽  
Author(s):  
H. Inokuchi ◽  
P. Hoben ◽  
F. Yamao ◽  
H. Ozeki ◽  
D. Soll

Author(s):  
Tatsuo Yanagisawa ◽  
Mitsuo Kuratani ◽  
Eiko Seki ◽  
Nobumasa Hino ◽  
Kensaku Sakamoto ◽  
...  

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