Mapping of the active site of Escherichia coli methionyl-tRNA synthetase: identification of amino acid residues labeled by periodate-oxidized tRNAfMet molecules having modified lengths at the 3'-acceptor end

Biochemistry ◽  
1990 ◽  
Vol 29 (35) ◽  
pp. 8190-8198 ◽  
Author(s):  
Codjo Hountondji ◽  
Jean Marie Schmitter ◽  
Christian Beauvallet ◽  
Sylvain Blanquet
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Active Site ◽  
Trna Synthetase ◽  
Amino Acid Residues ◽  
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 Identification of potential amino acid residues supporting anticodon recognition in yeast methionyl-tRNA synthetase

FEBS Letters ◽  
1991 ◽  
Vol 289 (2) ◽  
pp. 217-220 ◽  
Author(s):  
Laurence Despons ◽  
Philippe Walter ◽  
Bruno Senger ◽  
Jean-Pierre Ebel ◽  
Franco Fasiolo
Keyword(s):  
Amino Acid ◽  
Trna Synthetase ◽  
Amino Acid Residues ◽  
Methionyl Trna Synthetase

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.

scholarly journals Identification of amino acid residues at the active site of endosialidase that dissociate the polysialic acid binding and cleaving activities in Escherichia coli K1 bacteriophages

2007 ◽  
Vol 405 (3) ◽  
pp. 465-472 ◽  
Author(s):  
Elina Jakobsson ◽  
Anne Jokilammi ◽  
Juha Aalto ◽  
Pauli Ollikka ◽  
Jukka V. Lehtonen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Active Site ◽  
Structural Model ◽  
Polysialic Acid ◽  
Binding Activity ◽  
Enzymic Activity ◽  
Amino Acid Residues ◽  
Post Translational Modification ◽  
Escherichia Coli K1

Endosialidase (endo-N-acetylneuraminidase) is a tailspike enzyme of bacteriophages specific for human pathogenic Escherichia coli K1, which specifically recognizes and degrades polySia (polysialic acid). polySia is also a polysaccharide of the capsules of other meningitis- and sepsis-causing bacteria, and a post-translational modification of the NCAM (neural cell-adhesion molecule). We have cloned and sequenced three spontaneously mutated endosialidases of the PK1A bacteriophage and one of the PK1E bacteriophage which display lost or residual enzyme activity but retain the binding activity to polySia. Single to triple amino acid substitutions were identified, and back-mutation constructs indicated that single substitutions accounted for only partial reduction of enzymic activity. A homology-based structural model of endosialidase revealed that all substituted amino acid residues localize to the active site of the enzyme. The results reveal the importance of non-catalytic amino acid residues for the enzymatic activity. The results reveal the molecular background for the dissociation of the polySia binding and cleaving activities of endosialidase and for the evolvement of ‘host range’ mutants of E. coli K1 bacteriophages.

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