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Journal Abstract Search


147 related items for PubMed ID: 4581819

  • 1. The mechanism of action of methionyl-tRNA synthetase. 3. Ion requirements and kinetic parameters of the ATP-PPi exchange and methionine-transfer reactions catalyzed by the native and trypsin-modified enzymes.
    Lawrence F, Blanquet S, Poiret M, Robert-Gero M, Waller JP.
    Eur J Biochem; 1973 Jul 02; 36(1):234-43. PubMed ID: 4581819
    [No Abstract] [Full Text] [Related]

  • 2. The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. 1. Fluorescence studies on tRNAMet binding as a function of ligands, ions and pH.
    Blanquet S, Iwatsubo M, Waller JP.
    Eur J Biochem; 1973 Jul 02; 36(1):213-26. PubMed ID: 4581817
    [No Abstract] [Full Text] [Related]

  • 3. The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. Mechanism of the amino-acid activation reaction catalyzed by the native and the trypsin-modified enzymes.
    Blanquet S, Fayat G, Waller JP.
    Eur J Biochem; 1974 May 15; 44(2):343-51. PubMed ID: 4365501
    [No Abstract] [Full Text] [Related]

  • 4. The mechanism of action of methionyl-tRNA synthetase. 2. Interaction of the enzyme with specific and unspecific tRNAs.
    Blanquet S, Petrissant G, Waller JP.
    Eur J Biochem; 1973 Jul 02; 36(1):227-33. PubMed ID: 4581818
    [No Abstract] [Full Text] [Related]

  • 5. 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.
    Fayat G, Waller JP.
    Eur J Biochem; 1974 May 15; 44(2):335-42. PubMed ID: 4600363
    [No Abstract] [Full Text] [Related]

  • 6. Interrelation between transfer RNA and amino-acid-activating sites of methionyl transfer RNA synthetase from Escherichia coli.
    Jacques Y, Blanquet S.
    Eur J Biochem; 1977 Oct 03; 79(2):433-41. PubMed ID: 336359
    [Abstract] [Full Text] [Related]

  • 7. Couplings between the sites for methionine and adenosine 5'-triphosphate in the amino acid activation reaction catalyzed by trypsin-modified methionyl-transfer RNA synthetase from Escherichia coli.
    Fayat G, Fromant M, Blanquet S.
    Biochemistry; 1977 May 31; 16(11):2570-9. PubMed ID: 193563
    [No Abstract] [Full Text] [Related]

  • 8. The aminoacylation of transfer ribonucleic acid. Recognition of methionine by Escherichia coli methionyl-transfer ribonucleic acid synthetase.
    Old JM, Jones DS.
    Biochem J; 1977 Aug 01; 165(2):367-73. PubMed ID: 336037
    [Abstract] [Full Text] [Related]

  • 9. Methionyl-tRNA synthetase from Escherichia coli: substituting magnesium by manganese in the L-methionine activating reaction.
    Hyafil F, Blanquet S.
    Eur J Biochem; 1977 Apr 15; 74(3):481-93. PubMed ID: 323013
    [Abstract] [Full Text] [Related]

  • 10. The mechanism of action of methionyl-tRNA synthetase from Escherichia coli. Inhibition by adenosine and 8-aminoadenosine of the amino-acid activation reaction.
    Blanquet S, Fayat G, Poiret M, Waller JP.
    Eur J Biochem; 1975 Feb 21; 51(2):567-71. PubMed ID: 168070
    [Abstract] [Full Text] [Related]

  • 11. Methionyl-tRNA synthetase from Escherichia coli: active stoichiometry and stopped-flow analysis of methionyl adenylate formaiton.
    Hyafil F, Jacques Y, Fayat G, Fromant M, Dessen P, Blanquet S.
    Biochemistry; 1976 Aug 24; 15(17):3678-85. PubMed ID: 182214
    [Abstract] [Full Text] [Related]

  • 12. Enzymatic deacylation of methionyl-tRNAfMet catalysed by methionyl, isoleucyl and phenylalanyl-tRNA synthetases.
    Sourgoutchov A, Blanquet S, Fayat G, Waller JP.
    Eur J Biochem; 1974 Aug 01; 46(3):431-8. PubMed ID: 4604434
    [No Abstract] [Full Text] [Related]

  • 13. The role of polyamines in the aminoacyl transfer ribonucleic acid synthetase reactions. Demonstration of the requirement for magnesium ion and a secondary stimulatory effect of spermine.
    Santi DV, Webster RW.
    J Biol Chem; 1975 May 25; 250(10):3874-7. PubMed ID: 165187
    [Abstract] [Full Text] [Related]

  • 14. ATP-induced activation of the aminoacylation of tRNA by the isoleucyl-tRNA synthetase from Escherichia coli.
    Airas RK.
    Eur J Biochem; 1988 Sep 15; 176(2):359-63. PubMed ID: 3046945
    [Abstract] [Full Text] [Related]

  • 15. A stereochemical and positional isotope-exchange study of the mechanism of activation of methionine by methionyl-tRNA synthetase from Escherichia coli.
    Lowe G, Sproat BS, Tansley G.
    Eur J Biochem; 1983 Feb 01; 130(2):341-5. PubMed ID: 6337846
    [Abstract] [Full Text] [Related]

  • 16. Affinity labeling of aminoacyl-tRNA synthetases with adenosine triphosphopyridoxal: probing the Lys-Met-Ser-Lys-Ser signature sequence as the ATP-binding site in Escherichia coli methionyl-and valyl-tRNA synthetases.
    Hountondji C, Schmitter JM, Fukui T, Tagaya M, Blanquet S.
    Biochemistry; 1990 Dec 25; 29(51):11266-73. PubMed ID: 2271710
    [Abstract] [Full Text] [Related]

  • 17. Methionyl-tRNA synthetase from Escherichia coli. Inactivation and labeling by periodate-treated initiator tRNA.
    Fayat G, Hountondji C, Blanquet S.
    Eur J Biochem; 1979 May 02; 96(1):87-92. PubMed ID: 222589
    [Abstract] [Full Text] [Related]

  • 18. The amino acid activation reaction catalyzed by methionyl-transfer rna synthetase: evidence for synergistic coupling between the sites for methionine adenosine and pyrophosphate.
    Blanquet S, Fayat G, Waller JP.
    J Mol Biol; 1975 May 05; 94(1):1-15. PubMed ID: 167177
    [No Abstract] [Full Text] [Related]

  • 19. 31P NMR of the reversible methionine activation reaction catalyzed by methionyl-tRNA synthetase of Escherichia coli. Equilibrium, interconversion rates, and NMR parameters of the enzyme-bound species.
    Fayat G, Blanquet S, Nageswara Rao BD, Cohn M.
    J Biol Chem; 1980 Sep 10; 255(17):8164-9. PubMed ID: 6997291
    [No Abstract] [Full Text] [Related]

  • 20. Aminoacyl transfer RNA formation. II. Comparison of the mechanisms of aminoacylations stimulated by polyamines and Mg 2+ .
    Igarashi K, Matsuzaki K, Takeda Y.
    Biochim Biophys Acta; 1972 Apr 12; 262(4):476-87. PubMed ID: 4336270
    [No Abstract] [Full Text] [Related]


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