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Literature summary extracted from

  • Hadd, A.; Perona, J.J.
    Coevolution of specificity determinants in eukaryotic glutamyl- and glutaminyl-tRNA synthetases (2014), J. Mol. Biol., 426, 3619-3633 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.17 gene GUS1, phylogenetic analysis Saccharomyces cerevisiae
6.1.1.18 gene GLN4, phylogenetic analysis Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
6.3.5.7 additional information construction of an an N-terminal deletion mutant lacking amino acids 1-186 corresponding to the eukaryote-specific protein domains. The domains substantially influence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in either specific nucleotide readout or discrimination against noncognate tRNA Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.17 additional information
-
 additional information steady-state and transient kinetic analysis Saccharomyces cerevisiae
6.1.1.17 0.0012
-
 tRNAGlu pH and temperature not specified in the publication Saccharomyces cerevisiae
6.1.1.17 20
-
 L-glutamate pH and temperature not specified in the publication Saccharomyces cerevisiae
6.1.1.18 additional information
-
 additional information steady-state and transient kinetic analysis Saccharomyces cerevisiae
6.1.1.18 0.00019
-
 tRNAGln pH and temperature not specified in the publication Saccharomyces cerevisiae
6.1.1.18 1.7
-
 L-glutamine pH and temperature not specified in the publication Saccharomyces cerevisiae
6.3.5.7 0.16
-
 L-glutamine wild-type, pH 7.5, 37°C Saccharomyces cerevisiae
6.3.5.7 0.19
-
 L-glutamyl-tRNAGln wild-type, pH 7.5, 37°C Saccharomyces cerevisiae
6.3.5.7 1.2
-
 L-glutamine N-terminal deletion mutant, pH 7.5, 37°C Saccharomyces cerevisiae
6.3.5.7 5.6
-
 L-glutamyl-tRNAGln N-terminal deletion mutant, pH 7.5, 37°C Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.17 Mg2+ required Saccharomyces cerevisiae
6.1.1.18 Mg2+ required Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.17 ATP + L-glutamate + tRNAGlu Saccharomyces cerevisiae
-
 AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
6.1.1.17 ATP + L-glutamate + tRNAGlu Saccharomyces cerevisiae ATCC 204508 / S288c
-
 AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
6.1.1.18 ATP + L-glutamine + tRNAGln Saccharomyces cerevisiae
-
 AMP + diphosphate + L-glutaminyl-tRNAGln
-
 ?
6.1.1.18 ATP + L-glutamine + tRNAGln Saccharomyces cerevisiae ATCC 204508 / S288c
-
 AMP + diphosphate + L-glutaminyl-tRNAGln
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.17 Saccharomyces cerevisiae P46655
-
-
6.1.1.17 Saccharomyces cerevisiae ATCC 204508 / S288c P46655
-
-
6.1.1.18 Saccharomyces cerevisiae P13188
-
-
6.1.1.18 Saccharomyces cerevisiae ATCC 204508 / S288c P13188
-
-
6.3.5.7 Saccharomyces cerevisiae P13188
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.17 ATP + L-glutamate + tRNAGlu
-
 Saccharomyces cerevisiae AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
6.1.1.17 ATP + L-glutamate + tRNAGlu a two-step aminoacylation reaction Saccharomyces cerevisiae AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
6.1.1.17 ATP + L-glutamate + tRNAGlu
-
 Saccharomyces cerevisiae ATCC 204508 / S288c AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
6.1.1.17 ATP + L-glutamate + tRNAGlu a two-step aminoacylation reaction Saccharomyces cerevisiae ATCC 204508 / S288c AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?
6.1.1.18 ATP + L-glutamine + tRNAGln
-
 Saccharomyces cerevisiae AMP + diphosphate + L-glutaminyl-tRNAGln
-
 ?
6.1.1.18 ATP + L-glutamine + tRNAGln a two-step aminoacylation reaction Saccharomyces cerevisiae AMP + diphosphate + L-glutaminyl-tRNAGln
-
 ?
6.1.1.18 ATP + L-glutamine + tRNAGln
-
 Saccharomyces cerevisiae ATCC 204508 / S288c AMP + diphosphate + L-glutaminyl-tRNAGln
-
 ?
6.1.1.18 ATP + L-glutamine + tRNAGln a two-step aminoacylation reaction Saccharomyces cerevisiae ATCC 204508 / S288c AMP + diphosphate + L-glutaminyl-tRNAGln
-
 ?
6.3.5.7 ATP + L-glutamyl-tRNAGln + L-glutamine
-
 Saccharomyces cerevisiae ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
-
 ?
6.3.5.7 ATP + L-glutamyl-tRNAGln + L-glutamine
-
 Saccharomyces cerevisiae ATCC 204508 / S288c ADP + phosphate + L-glutaminyl-tRNAGln + L-glutamate
-
 ?

Subunits

EC Number Subunits Comment Organism
6.1.1.18 More Saccharomyces cerevisiae GlnRS contains an N-terminal domain that is conserved in eukaryotic enzymes and is not present in bacterial homologues, The N-terminal domain consists of 187 amino acids organized in two helical subdomains and is followed by an unstructured 26-residue linker that links it with the main catalytic portion of the enzyme, the C-terminal domain, computational modeling Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
6.1.1.17 discriminating GluRS
-
 Saccharomyces cerevisiae
6.1.1.17 GluRS
-
 Saccharomyces cerevisiae
6.1.1.17 glutamyl-tRNAsynthetase
-
 Saccharomyces cerevisiae
6.1.1.18 GlnRS
-
 Saccharomyces cerevisiae
6.1.1.18 Glutaminyl-tRNA synthetase
-
 Saccharomyces cerevisiae
6.3.5.7 Gln4
-
 Saccharomyces cerevisiae
6.3.5.7 GlnRS
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.17 1.5
-
 L-glutamate pH and temperature not specified in the publication Saccharomyces cerevisiae
6.1.1.17 1.5
-
 tRNAGlu pH and temperature not specified in the publication Saccharomyces cerevisiae
6.1.1.18 1.4
-
 L-glutamine pH and temperature not specified in the publication Saccharomyces cerevisiae
6.1.1.18 1.4
-
 tRNAGln pH and temperature not specified in the publication Saccharomyces cerevisiae
6.3.5.7 1.4
-
 L-glutamine wild-type, pH 7.5, 37°C Saccharomyces cerevisiae
6.3.5.7 1.7
-
 L-glutamine N-terminal deletion mutant, pH 7.5, 37°C Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.17 ATP
-
 Saccharomyces cerevisiae
6.1.1.18 ATP
-
 Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
6.1.1.17 evolution the enzyme evolved by gene duplication in early eukaryotes from a nondiscriminating glutamyl-tRNAsynthetase (GluRSND, EC 6.1.1.24) that aminoacylates both tRNAGln and tRNAGlu with glutamate. This ancient GluRS also separately differentiated to exclude tRNAGln as a substrate, and the resulting discriminating GluRS and GlnRS further acquired additional protein domains assisting function in cis (the GlnRS N-terminal Yqey domain) or in trans (the Arc1p protein associating with GluRS), evolutionary modeling, detailed overview. These added domains are absent in contemporary bacterial GlnRS and GluRS. The eukaryote-specific protein domains substantially influence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in either specific nucleotide readout or discrimination against noncognate tRNA. Eukaryotic tRNAGln and tRNAGlu recognition determinants are found in equivalent positions and aremutually exclusive to a significant degree, with key nucleotides located adjacent to portions of the protein structure that differentiated during the evolution of archaeal nondiscriminating GluRS to GlnRS. The added eukaryotic domains arose in response to distinctive selective pressures associated with the greater complexity of the eukaryotic translational apparatus. The affinity of GluRS for glutamate is significantly increased when Arc1p is not associated with the enzyme. GluRS and GlnRS are among just four aaRS families (the others are arginyl-tRNA synthetase and class I LysRS) that require the presence of tRNA for synthesis of the aminoacyl adenylate reaction intermediate. Each cytoplasmic GlxRS-tRNA pair has fully lost the ancestral nondiscriminating activity in the course of coevolution, and the more stringent specificities of Saccharomyces cerevisiae GlnRS and GluRS arise from the conserved catalytic portions of each enzyme Saccharomyces cerevisiae
6.1.1.17 additional information analysis of the contributions to aminoacylation efficiency made by the N-terminal Arc1p domain of Saccharomyces cerevisiae GluRS. tRNA recognition determinants in the acceptor arm, at the 3'-anticodon position and in the globular core, overview, overview Saccharomyces cerevisiae
6.1.1.18 evolution the enzyme evolved by gene duplication in early eukaryotes from a nondiscriminating glutamyl-tRNAsynthetase (GluRSND, EC 6.1.1.24) that aminoacylates both tRNAGln and tRNAGlu with glutamate. This ancient GluRS also separately differentiated to exclude tRNAGln as a substrate, and the resulting discriminating GluRS and GlnRS further acquired additional protein domains assisting function in cis (the GlnRS N-terminal Yqey domain) or in trans (the Arc1p protein associating with GluRS), evolutionary modeling, detailed overview. These added domains are absent in contemporary bacterial GlnRS and GluRS. The eukaryote-specific protein domains substantially influence amino acid binding, tRNA binding and aminoacylation efficiency, but they play no role in either specific nucleotide readout or discrimination against noncognate tRNA. Eukaryotic tRNAGln and tRNAGlu recognition determinants are found in equivalent positions and aremutually exclusive to a significant degree, with key nucleotides located adjacent to portions of the protein structure that differentiated during the evolution of archaeal nondiscriminating GluRS to GlnRS. The added eukaryotic domains arose in response to distinctive selective pressures associated with the greater complexity of the eukaryotic translational apparatus. GluRS and GlnRS are among just four aaRS families (the others are arginyl-tRNA synthetase and class I LysRS) that require the presence of tRNA for synthesis of the aminoacyl adenylate reaction intermediate. Each cytoplasmic GlxRS-tRNA pair has fully lost the ancestral nondiscriminating activity in the course of coevolution, and the more stringent specificities of Saccharomyces cerevisiae GlnRS and GluRS arise from the conserved catalytic portions of each enzyme Saccharomyces cerevisiae
6.1.1.18 additional information analysis of the contributions to aminoacylation efficiency made by the N-terminal Yqey domain of Saccharomyces cerevisiae GlnRS. tRNA recognition determinants in the acceptor arm, at the 3'-anticodon position and in the globular core, overview Saccharomyces cerevisiae
6.3.5.7 metabolism eukaryotic tRNAGln and tRNAGlu recognition determinants are found in equivalent positions of glutaminyl-tRNA synthetase and glutamyl-tRNA synthetase, respectively, and are mutually exclusive to a significant degree, with key nucleotides located adjacent to portions of the protein structure that differentiated during the evolution of archaeal nondiscriminating luRS to GlnRS Saccharomyces cerevisiae

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.1.1.17 0.824
-
 L-glutamate pH and temperature not specified in the publication Saccharomyces cerevisiae
6.1.1.17 1250
-
 tRNAGlu pH and temperature not specified in the publication Saccharomyces cerevisiae
6.1.1.18 0.824
-
 L-glutamine pH and temperature not specified in the publication Saccharomyces cerevisiae
6.1.1.18 7368.4
-
 tRNAGln pH and temperature not specified in the publication Saccharomyces cerevisiae
6.3.5.7 1.4
-
 L-glutamine wild-type, pH 7.5, 37°C Saccharomyces cerevisiae
6.3.5.7 1.7
-
 L-glutamine N-terminal deletion mutant, pH 7.5, 37°C Saccharomyces cerevisiae