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 | 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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Pseudomonas aeruginosa |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Pseudomonas aeruginosa |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas aeruginosa | - |
- |
- |
Pseudomonas aeruginosa | - |
gene aspS | - |
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 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 | 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 | Comment | Organism |
---|---|---|
Aspartyl-tRNA synthetase | - |
Pseudomonas aeruginosa |
nondiscriminating AspRS | - |
Pseudomonas aeruginosa |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Pseudomonas aeruginosa |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Pseudomonas aeruginosa |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Pseudomonas aeruginosa |