Crystallographic study at 2·5 Å resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP

1990 ◽  
Vol 216 (2) ◽  
pp. 411-424 ◽  
Author(s):  
S. Brunie ◽  
C. Zelwer ◽  
J.-L. Risler
Keyword(s):  
Escherichia Coli ◽  
Trna Synthetase ◽  
Crystallographic Study ◽  
Methionyl Trna Synthetase

scholarly journals Use of β3-methionine as an amino acid substrate of Escherichia coli methionyl-tRNA synthetase

2020 ◽  
Vol 209 (2) ◽  
pp. 107435 ◽  
Author(s):  
Giuliano Nigro ◽  
Sophie Bourcier ◽  
Christine Lazennec-Schurdevin ◽  
Emmanuelle Schmitt ◽  
Philippe Marlière ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Trna Synthetase ◽  
Methionyl Trna Synthetase ◽  
Acid Substrate ◽  
Amino Acid Substrate

scholarly journals Methionyl-tRNA Synthetase from Escherichia coli

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

A new method for the isolation of methionyl transfer RNA synthetase mutants from Escherichia coli

1975 ◽  
Vol 21 (6) ◽  
pp. 754-758 ◽  
Author(s):  
John B. Armstrong ◽  
John A. Fairfield
Keyword(s):  
Escherichia Coli ◽  
Trna Synthetase ◽  
Transfer Rna ◽  
New Method ◽  
Wild Type ◽  
E Coli ◽  
Adenosyl Methionine ◽  
K 12 ◽  
Methionyl Trna Synthetase

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.

scholarly journals The aminoacylation of transfer ribonucleic acid. Recognition of methionine by Escherichia coli methionyl-transfer ribonucleic acid synthetase

1977 ◽  
Vol 165 (2) ◽  
pp. 367-373 ◽  
Author(s):  
J M Old ◽  
D S Jones
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Ribonucleic Acid ◽  
Chemical Nature ◽  
Trna Synthetase ◽  
Side Chain ◽  
Amino Acid Side Chain ◽  
Sulphur Atom ◽  
Recognition Mechanism ◽  
Methionyl Trna Synthetase

The mechanism of the recognition of methionine by Escherichia coli methionyl-tRNA synthetase was examined by a kinetic study of the recognition of methionine analogues in the ATP-PPi exchange reaction and the tRNA-aminoacylation reaction. The results show that the recognition mechanism consists of three parts: (1) the recognition of the size, shape and chemical nature of the amino acid side chain at the methionine-binding stage of the reaction; (2) the recognition of the length of the side chain at the stage of aminoacyl-adenylate complex-formation; (3) the recognition of the sulphur atom in the side chain at the stage of methionyl-tRNA formation. It is proposed that the sulphur atom interacts with the enzyme to induce a conformational change. A model of the active site incorporating the mechanism of methionine recognition is presented.

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