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Literature summary for 6.1.1.23 extracted from
- Two residues in the anticodon recognition domain of the aspartyl-tRNA synthetase from Pseudomonas aeruginosa are individually implicated in the recognition of tRNAAsn (2006), J. Bacteriol., 188, 269-274.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene aspS, DNA and amino acid sequence determination and analysis, expression of His-tagged wild-type and mutant enzymes | Pseudomonas aeruginosa |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| G83K | aspartylation reaction of the mutant enzyme is 55% as fast as the wild-type enzyme | Pseudomonas aeruginosa |
| G83K | site-directed mutagenesis, the mutation increases the specificity of tRNAAsp charging over that of tRNAAsn by 4.2fold | Pseudomonas aeruginosa |
| H31L | aspartylation reaction of the mutant enzyme is 84% as fast as the wild-type enzyme | Pseudomonas aeruginosa |
| H31L | aspartylation reaction of the mutant enzyme is 92% as fast as the wild-type enzyme | Pseudomonas aeruginosa |
| H31L | site-directed mutagenesis, the mutation increases the specificity of tRNAAsp charging over that of tRNAAsn by 3.5fold | Pseudomonas aeruginosa |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | - |
Pseudomonas aeruginosa |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Pseudomonas aeruginosa |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-aspartate + tRNAAsn | Pseudomonas aeruginosa | - |
AMP + diphosphate + aspartyl-tRNAAsn | - |
? | |
| ATP + L-aspartate + tRNAAsp | Pseudomonas aeruginosa | - |
AMP + diphosphate + aspartyl-tRNAAsp | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas aeruginosa | - |
- |
- |
| Pseudomonas aeruginosa | - |
gene aspS | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + L-aspartate + tRNAAsx = AMP + diphosphate + L-aspartyl-tRNAAsx | residues H31 and G83 are important determinants for substrate specificity towards tRNA substrates, molecular modeling | Pseudomonas aeruginosa |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
activities of wild-type and mutant enzymes with different tRNA substrates | Pseudomonas aeruginosa |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-aspartate + tRNAAsn | two residues in the anticodon recognition domain of the aspartyl-tRNA synthetase, H31 and G83, are individually implicated in the recognition of tRNAAsn | Pseudomonas aeruginosa | AMP + diphosphate + L-aspartyl-tRNAAsn | - |
? | |
| ATP + L-aspartate + tRNAAsn | - |
Pseudomonas aeruginosa | AMP + diphosphate + aspartyl-tRNAAsn | - |
? | |
| ATP + L-aspartate + tRNAAsn | tRNA substrate from Escherichia coli | Pseudomonas aeruginosa | AMP + diphosphate + aspartyl-tRNAAsn | - |
? | |
| ATP + L-aspartate + tRNAAsp | - |
Pseudomonas aeruginosa | AMP + diphosphate + aspartyl-tRNAAsp | - |
? | |
| ATP + L-aspartate + tRNAAsp | tRNA substrate from Escherichia coli | Pseudomonas aeruginosa | AMP + diphosphate + aspartyl-tRNAAsp | - |
? | |
| additional information | two residues in the anticodon recognition domain of the enzyme are individually implicated in the recognition of tRNAAsn, nondiscriminating AspRSs possess a histidine at position 31 and usually a glycine at position 83, whereas discriminating AspRSs, EC 6.1.1.12, possess a leucine at position 31 and a residue other than a glycine at position 83 | Pseudomonas aeruginosa | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Aspartyl-tRNA synthetase | - |
Pseudomonas aeruginosa |
| nondiscriminating AspRS | - |
Pseudomonas aeruginosa |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Pseudomonas aeruginosa |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Pseudomonas aeruginosa |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Pseudomonas aeruginosa | |
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Release 2023.1 (January 2023)
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