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Glutamyl-tRNA sythetase.
Freist W, Gauss DH, Söll D, Lapointe J. Freist W, et al. Among authors: lapointe j. Biol Chem. 1997 Nov;378(11):1313-29. Biol Chem. 1997. PMID: 9426192 Review.
The monomeric glutamyl-tRNA synthetase of Escherichia coli. Purification and relation between its structural and catalytic properties.
Kern D, Potier S, Boulanger Y, Lapointe J. Kern D, et al. Among authors: lapointe j. J Biol Chem. 1979 Jan 25;254(2):518-24. J Biol Chem. 1979. PMID: 368055 Free article.
It is a monomer with a molecular weight of 56,000 and has the same kinetic properties as those of the alpha chain of the dimeric alphabeta-glutamyl-tRNA synthetase described previously (Lapointe, J., and Soll, D. (1972) J. Biol. Chem. 247, 4966-4974). It is t …
It is a monomer with a molecular weight of 56,000 and has the same kinetic properties as those of the alpha chain of the dimeric alphabeta-g …
The zinc-binding site of Escherichia coli glutamyl-tRNA synthetase is located in the acceptor-binding domain. Studies by extended x-ray absorption fine structure, molecular modeling, and site-directed mutagenesis.
Liu J, Gagnon Y, Gauthier J, Furenlid L, L'Heureux PJ, Auger M, Nureki O, Yokoyama S, Lapointe J. Liu J, et al. Among authors: lapointe j. J Biol Chem. 1995 Jun 23;270(25):15162-9. doi: 10.1074/jbc.270.25.15162. J Biol Chem. 1995. PMID: 7797500 Free article.
The zinc contents of fragments of Escherichia coli glutamyl-tRNA synthetase, as well as the conservation of the CYC sequence only in zinc-containing glutamyl-tRNA synthetases, suggested that the 98CYCX24-CRHSHEHHADDEPC138 includes some or all residues involved in binding its zinc …
The zinc contents of fragments of Escherichia coli glutamyl-tRNA synthetase, as well as the conservation of the CYC sequence only in zinc-co …
536 results