Literature DB >> 4600363

The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. Equilibrium-dialysis studies on the binding of methionine, ATP and ATP-Mg2+ by the native and trypsin-modified enzymes.

G Fayat, J P Waller.   

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Year:  1974        PMID： 4600363     DOI： 10.1111/j.1432-1033.1974.tb03490.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN： 0014-2956


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  4 in total

1.  Enhanced level and metabolic regulation of methionyl-transfer ribonucleic acid synthetase in different strains of Escherichia coli K-12.

Authors:  D Cassio; Y Mathien; J P Waller
Journal:  J Bacteriol       Date:  1975-08       Impact factor: 3.490

2.  Aminoacyl-tRNA synthetases: affinity labeling of the ATP binding site by 2', 3' -ribose oxidized ATP.

Authors:  G Fayat; M Fromant; S Blanquet
Journal:  Proc Natl Acad Sci U S A       Date:  1978-05       Impact factor: 11.205

3.  Adenosine conformations of nucleotides bound to methionyl tRNA synthetase by transferred nuclear Overhauser effect spectroscopy.

Authors:  N Murali; Y Lin; Y Mechulam; P Plateau; B D Rao
Journal:  Biophys J       Date:  1997-05       Impact factor: 4.033

4.  Metal-binding site in a class I tRNA synthetase localized to a cysteine cluster inserted into nucleotide-binding fold.

Authors:  J A Landro; P Schimmel
Journal:  Proc Natl Acad Sci U S A       Date:  1993-03-15       Impact factor: 11.205
  4 in total

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