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2 negative charge on the phosphorus center of glutaminyl-adenylate plays an important role in the tigh
4 Ks evolved from a common ancestor related to glutaminyl aminoacyl-tRNA synthetases, which may have be
5 for measurement of the deamidation rates of glutaminyl and asparaginyl residues in peptides and prot
6 The spontaneous nonenzymatic deamidation of glutaminyl and asparaginyl residues of peptides and prot
7 iscussed with respect to the hypothesis that glutaminyl and asparaginyl residues serve, through deami
9 formation of amide bonds between endo-gamma-glutaminyl and endo-epsilon-lysyl residues of proteins,
10 transglutaminase-catalyzed reaction between glutaminyl and lysyl side-chains, leading to a covalent
11 y are responsible for essentially all of the glutaminyl- and glutamyl-tRNA synthetase activity detect
19 in vitro expanded polyglutamine repeats are glutaminyl-donor substrates of tissue transglutaminase (
20 ign and synthesis of dipeptidyl N,N-dimethyl glutaminyl fluoromethyl ketones (fmk) as severe acute re
21 terial peptidoglycan contains L-alanyl-D-iso-glutaminyl-meso-diaminopimelyl-D-alanyl-D-alanine peptid
23 vacuolar SNAREs requires the wild-type three glutaminyl (Q) and one arginyl (R) residues for optimal
26 e can also form ester bonds between specific glutaminyl residues of human involucrin and a synthetic
27 CheD catalyzes amide hydrolysis of specific glutaminyl side chains of the B. subtilis chemoreceptor
28 hylaminonaphthalene sulfonyl)diamidopentane (glutaminyl substrate) is cross-linked to dansyl cadaveri
29 is (glutamyl-prolyl-transfer RNA synthetase, glutaminyl-transfer RNA synthetase, elongation factor 2,
30 ombination of discriminating asparaginyl and glutaminyl tRNA synthetase (AARS) together with the amid
31 base frequencies for the seryl, aspartyl and glutaminyl tRNA-synthetase and U1 RNA-protein complexes.
34 synthetase to synthesize Glu-tRNA(Gln) and a glutaminyl-tRNA amidotransferase to convert Glu-tRNA(Gln
35 alysis of the x-ray crystal structure of the glutaminyl-tRNA aminoacyl synthetase (GlnRS)-tRNA2Gln co
36 y prokaryotes form the amide aminoacyl-tRNAs glutaminyl-tRNA and asparaginyl-tRNA by tRNA-dependent a
37 "21st synthetase-tRNA pairs" include E. coli glutaminyl-tRNA synthetase (GlnRS) along with an amber s
38 ependent on coexpression of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) along with the E. col
39 e free state, and for tRNAGln complexed with glutaminyl-tRNA synthetase (GlnRS) are in good agreement
42 alter amino acid specificities of TrpRS and glutaminyl-tRNA synthetase (GlnRS) by mutagenesis withou
46 alysis of aminoacylation of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) has revealed that the
47 due from glutamyl-tRNA synthetase (GluRS) to glutaminyl-tRNA synthetase (GlnRS) improves the K(M) of
49 in the crystal structure of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) in complex with tRNAG
53 previously described mutant Escherichia coli glutaminyl-tRNA synthetase (GlnRS) proteins that incorre
54 eady-state and transient kinetic analyses of glutaminyl-tRNA synthetase (GlnRS) reveal that the enzym
55 rom the catalytic domain of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) were replaced with th
56 karyotes and some bacteria employ a specific glutaminyl-tRNA synthetase (GlnRS) which other Bacteria,
57 nthesis, which in eukaryotes is catalyzed by glutaminyl-tRNA synthetase (GlnRS), while most bacteria,
58 aminoacyl-tRNA synthetase, including E. coli glutaminyl-tRNA synthetase (GlnRS), yet functions with t
64 dentification of mutations in QARS (encoding glutaminyl-tRNA synthetase [QARS]) as the causative vari
65 -tRNAGln, functionally replacing the lack of glutaminyl-tRNA synthetase activity in Gram-positive eub
68 eria lack genes encoding asparaginyl- and/or glutaminyl-tRNA synthetase and consequently rely on an i
69 ecific interactions between Escherichia coli glutaminyl-tRNA synthetase and tRNA(Gln) have been shown
72 undwork for the acquisition of the canonical glutaminyl-tRNA synthetase by lateral gene transfer from
74 dy-state kinetic studies of Escherichia coli glutaminyl-tRNA synthetase conclusively demonstrate the
75 d that residues Asp66, Tyr211, and Phe233 in glutaminyl-tRNA synthetase could potentially facilitate
76 either the cytoplasmic nor the mitochondrial glutaminyl-tRNA synthetase distinguishes between the imp
77 y perturb the enzyme-tRNA interface, E. coli glutaminyl-tRNA synthetase does not charge yeast tRNA.
80 ells by regulating expression of the E. coli glutaminyl-tRNA synthetase gene in an inducible, cell-ty
83 2.5 A crystal structure of Escherichia coli glutaminyl-tRNA synthetase in a quaternary complex with
86 gical activity of an essential RNA.Bacterial glutaminyl-tRNA synthetase poorly aminoacylates yeast tR
87 structure of the complex between tRNAGln and glutaminyl-tRNA synthetase shows that the enzyme interac
88 gly, T. brucei uses the same eukaryotic-type glutaminyl-tRNA synthetase to form mitochondrial and cyt
89 dues were randomly mutated and the resulting glutaminyl-tRNA synthetase variants were screened in viv
91 A is dependent upon the expression of E.coli glutaminyl-tRNA synthetase, indicating that none of the
92 nsamidation, and the eukaryal cytoplasm uses glutaminyl-tRNA synthetase, it appears that the three do
93 The monomeric yeast Saccharomyces cerevisiae glutaminyl-tRNA synthetase, like several other class I e
95 inoacylated in vitro by the Escherichia coli glutaminyl-tRNA synthetase, suggesting that the lack of
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