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Journal Abstract Search
163 related items for PubMed ID: 4361287
1. The effect of adenosine analogues on the ATP-pyrophosphate exchange reaction catalysed by methionyl-tRNA synthetase. Lawrence F, Shire DJ, Waller JP. Eur J Biochem; 1974 Jan 03; 41(1):73-81. PubMed ID: 4361287 [No Abstract] [Full Text] [Related]
2. 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]
3. Human tryptophanyl transfer ribonucleic acid synthetase. Comparison of the kinetic mechanism to that of the Escherichia coli tryptophanyl transfer ribonucleic acid synthetase. Penneys NS, Muench KH. Biochemistry; 1974 Jan 29; 13(3):566-71. PubMed ID: 4358952 [No Abstract] [Full Text] [Related]
4. Kinetics of pyrophosphate-ATP exchange catalysed by L-tryptophan: tRNA ligase from Escherichia coli. Penzer GR, Plumbridge JA. Eur J Biochem; 1974 Jun 01; 45(1):291-5. PubMed ID: 4371652 [No Abstract] [Full Text] [Related]
5. Phenylalanyl-tRNA synthetase from Escherichia coli K10. Synergistic coupling between the sites for binding of L-phenylalanine and ATP. Kosakowski HM, Holler E. Eur J Biochem; 1973 Oct 05; 38(2):274-82. PubMed ID: 4359386 [No Abstract] [Full Text] [Related]
6. Kinetic scheme and kinetic parameters of the exchange of ATP-32P-pyrophosphates, catalyzed by tryptophanyl-tRNA synthetase from beef pancreas. Zinov'ev VV, Kiselev LL, Knorre DG, Kochkina LL, Malygin EG, Slin'ko MG, Timoshenko VI, Favorova OO. Mol Biol; 1974 Nov 05; 8(3):303-10. PubMed ID: 4373648 [No Abstract] [Full Text] [Related]
7. Fluorinated tryptophans as substrates and inhibitors of the ATP--(32P)PPi exchange reaction catalysed by tryptophanyl tRNA synthetase. Nevinsky GA, Favorova OO, Lavrik OI, Petrova TD, Kochkina LL, Savchenko TI. FEBS Lett; 1974 Jul 15; 43(2):135-8. PubMed ID: 4152887 [No Abstract] [Full Text] [Related]
8. 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]
9. 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]
10. Phenylalanyl transfer ribonucleic acid synthetase from Escherichia coli. Analysis of the adenosine triphosphate binding site. Santi DV, Danenberg PV, Montgomery KA. Biochemistry; 1971 Dec 07; 10(25):4821-4. PubMed ID: 4334587 [No Abstract] [Full Text] [Related]
11. [The formation of ATP from adenosine 5'-phosphoroimidazolide and pyrophosphate catalyzed by valyl-tRNA-synthetase]. Biriukov AI, Osipova TI, Khomutov RM. Biokhimiia; 1976 Oct 07; 41(10):1905-6. PubMed ID: 192333 [Abstract] [Full Text] [Related]
12. Role of the beta-phosphate-gamma-phosphate interchange reaction of adenosine triphosphate in amino acid discrimination by valyl- and methionyl-tRNA synthetases from Escherichia coli. Smith LT, Cohn M. Biochemistry; 1981 Jan 20; 20(2):385-91. PubMed ID: 6258639 [No Abstract] [Full Text] [Related]
13. 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]
14. 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]