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Glutamyl-tRNA

Structure of glutamyl-tRNA synthetase Catalyzing the first step of the indirect pathway 391... [Pg.383]

Indirect Pathway Inhibitors of Glutamyl-tRNA Synthetase, Aspartyl-tRNA... [Pg.384]

Figure 2 Indirect pathway for Asn-tRNA " and Gln-tRNA° " biosynthesis. ND-AspRS, nondiscriminating aspartyl-tRNA synthetase ND-GluRS, nondiscriminating glutamyl-tRNA systhetase AdT, aminoacyl-tRNA amidotransferase. Figure 2 Indirect pathway for Asn-tRNA " and Gln-tRNA° " biosynthesis. ND-AspRS, nondiscriminating aspartyl-tRNA synthetase ND-GluRS, nondiscriminating glutamyl-tRNA systhetase AdT, aminoacyl-tRNA amidotransferase.
Table 3 Inhibitors of glutamyl-tRNA synthetase (GluRS)... Table 3 Inhibitors of glutamyl-tRNA synthetase (GluRS)...
E. Verkamp A. M. Kumar A. Lloyd O. Martins N. Stange-Thomann D. Soil, Glutamyl-tRNA as an Intermediate in Glutamate Conversions. In tRNA Structure, Biosynthesis, and Function D. Soil, U. L. RajBhandary, Eds. American Society for Microbiology Washington, DC, 1995 pp 545-550. [Pg.425]

This enzyme catalyzes the ATP-dependent reaction of glutamyl-tRNA° " with glutamine to produce glutami-nyl-tRNA° ", ADP, orthophosphate, and glutamate. [Pg.317]

This enzyme [EC 6.1.1.17], also known as gluta-mate tRNA ligase, catalyzes the reaction of L-glutamate with tRNA° and ATP to produce L-glutamyl-tRNA° , AMP, and pyrophosphate. [Pg.317]

Solvent-accessible surface representation of the GlnRS enzyme complexed with tRNA and ATP. The region of contact between tRNA and protein extends across one side of the entire enzyme surface and includes interactions from all four protein domains. The acceptor end of the tRNA and the ATP are seen in the bottom of the deep cleft. Protein is inserted between the 5 and 3 ends of the tRNA and disrupts the expected base pair between Ul and A72. (From M. G. Rould, J. J. Persona, D. Soil, and T. Steitz, Structure of E. coli glutamyl-tRNA synthetics complexed with tRNA ln and ATP at 2.8-A resolution, implications for tRNA discrimination, Science 246 1135-1142, 1989, 1989 by the AAAS.)... [Pg.745]

Luque, L, Contreras, A., Zabulon, G., Herrero, A., and Houmard, J. (2002). Expression of the glutamyl-tRNA synthetase gene from the cyanobacterium Synechococcus sp PCC 7942 depends on nitrogen availability and the global regulator NtcA. Mol. Microbiol. 46, 1157—1167. [Pg.1337]

Figure 2 Biosynthesis of tetrapyrroles. 10, succinyl-CoA 11, glycine 12, 5-aminolevulinic acid 13, glutamyl-tRNA 14, porphobilinogen 15, hydroxymethylbilane 16, uroporphyrinogen III 17, chlorophyll a 18, heme a 19, coenzyme F430 20, vitamin 8 2 21, coenzyme... Figure 2 Biosynthesis of tetrapyrroles. 10, succinyl-CoA 11, glycine 12, 5-aminolevulinic acid 13, glutamyl-tRNA 14, porphobilinogen 15, hydroxymethylbilane 16, uroporphyrinogen III 17, chlorophyll a 18, heme a 19, coenzyme F430 20, vitamin 8 2 21, coenzyme...
Hungerer C, Weiss DS, Thauer RK, Jahn D. The hemA gene encoding glutamyl-tRNA reductase from the archaeon Methanobacterium thermoautotrophicum strain Marburg. Bioorg. Med. Chem. 1996 4 1089-1095. [Pg.680]

In plants and some bacterial species, ALA is synthesized from glutamate in a process involving glutamyl tRNA. Refer to Chapter 17 for a discussion of tRNA (transfer RNA). [Pg.500]

Glutamyl-tRNA Reductase and Glutamate-1 -Semialdehyde-2,1 -Aminomutase 449... [Pg.445]

V. Lakshman, P.G. Schultz, An archaebacteria-derived glutamyl-tRNA synthetase and tRNA pair for unnatural amino acid mutagenesis of proteins in Escherichia coli, Nucleic Acids Res. 2003, 31, 6700-6709. [Pg.294]


See other pages where Glutamyl-tRNA is mentioned: [Pg.35]    [Pg.106]    [Pg.385]    [Pg.392]    [Pg.393]    [Pg.393]    [Pg.393]    [Pg.396]    [Pg.414]    [Pg.424]    [Pg.317]    [Pg.317]    [Pg.746]    [Pg.855]    [Pg.855]    [Pg.526]    [Pg.527]    [Pg.247]    [Pg.267]    [Pg.500]    [Pg.727]    [Pg.295]    [Pg.295]    [Pg.448]    [Pg.449]    [Pg.449]    [Pg.451]    [Pg.854]    [Pg.855]    [Pg.855]    [Pg.855]    [Pg.164]    [Pg.218]   
See also in sourсe #XX -- [ Pg.497 ]




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