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Literature summary for 6.1.1.17 extracted from
- Coevolution of specificity determinants in eukaryotic glutamyl- and glutaminyl-tRNA synthetases (2014), J. Mol. Biol., 426, 3619-3633 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene GUS1, phylogenetic analysis | Saccharomyces cerevisiae |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | steady-state and transient kinetic analysis | Saccharomyces cerevisiae | |
| 0.0012 | - |
tRNAGlu | pH and temperature not specified in the publication | Saccharomyces cerevisiae |  |
| 20 | - |
L-glutamate | pH and temperature not specified in the publication | Saccharomyces cerevisiae | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Saccharomyces cerevisiae | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-glutamate + tRNAGlu | Saccharomyces cerevisiae | - |
AMP + diphosphate + L-glutamyl-tRNAGlu | - |
? | |
| ATP + L-glutamate + tRNAGlu | Saccharomyces cerevisiae ATCC 204508 / S288c | - |
AMP + diphosphate + L-glutamyl-tRNAGlu | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | P46655 | - |
- |
| Saccharomyces cerevisiae ATCC 204508 / S288c | P46655 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-glutamate + tRNAGlu | - |
Saccharomyces cerevisiae | AMP + diphosphate + L-glutamyl-tRNAGlu | - |
? | |
| ATP + L-glutamate + tRNAGlu | a two-step aminoacylation reaction | Saccharomyces cerevisiae | AMP + diphosphate + L-glutamyl-tRNAGlu | - |
? | |
| ATP + L-glutamate + tRNAGlu | - |
Saccharomyces cerevisiae ATCC 204508 / S288c | AMP + diphosphate + L-glutamyl-tRNAGlu | - |
? | |
| ATP + L-glutamate + tRNAGlu | a two-step aminoacylation reaction | Saccharomyces cerevisiae ATCC 204508 / S288c | AMP + diphosphate + L-glutamyl-tRNAGlu | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| discriminating GluRS | - |
Saccharomyces cerevisiae |
| GluRS | - |
Saccharomyces cerevisiae |
| glutamyl-tRNAsynthetase | - |
Saccharomyces cerevisiae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.5 | - |
L-glutamate | pH and temperature not specified in the publication | Saccharomyces cerevisiae | |
| 1.5 | - |
tRNAGlu | pH and temperature not specified in the publication | Saccharomyces cerevisiae | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Saccharomyces cerevisiae | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.824 | - |
L-glutamate | pH and temperature not specified in the publication | Saccharomyces cerevisiae | |
| 1250 | - |
tRNAGlu | pH and temperature not specified in the publication | Saccharomyces cerevisiae | |
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