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Literature summary for 6.1.1.9 extracted from
- Transfer RNA determinants for translational editing by Escherichia coli valyl-tRNA synthetase (2002), Nucleic Acids Res., 30, 2538-2545.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | stimulatory effects of diverse tRNA variants on the editing activity, overview | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | substitution of base 75 of C by U or A leads to effective stimulation of the editing activity at lower rates, substitution with G leads to reduction of the editing activity by 95%, mutational exchange of the discriminator base A73 to U73 or C73 does not alter enzyme activity but exchange to G73 stimulates editing activity of the catalytically inactive mutant | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-valine + tRNAVal | Escherichia coli | - |
AMP + diphosphate + L-valyl-tRNAVal | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal | substrate binding mechanism, bases A73 and C75 are involved in the tRNA substrate recognition and editing reaction | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-threonine + tRNAVal | 1 step performance of an originally two-step reaction, the enzyme can hardly differentiate between the cognate amino acid valine and others, especially threonine, to minimize misaminoacetylation the enzyme performs a proofreading, socalled editing reaction at a second active site, which is dependent on the presence of cognate tRNAVal whose 3'-end is involved in the editing reaction, a majority of editing by the enzyme entails prior charging of the tRNA, misacylated tRNA is a transient intermediate in the editing reaction | Escherichia coli | ? | - |
? | |
| ATP + L-valine + tRNAVal | - |
Escherichia coli | AMP + diphosphate + L-valyl-tRNAVal | - |
? | |
| ATP + L-valine + tRNAVal | two-step reaction, the enzyme can hardly differentiate between the cognate amino acid valine and others, especially threonine, to minimize misaminoacetylation the enzyme performs a proofreading, socalled editing reaction at a second active site, which is dependent on the presence of cognate tRNAVal whose 3'-end is involved in the editing reaction, a majority of editing by the enzyme entails prior charging of the tRNA, misacylated tRNA is a transient intermediate in the editing reaction | Escherichia coli | AMP + diphosphate + L-valyl-tRNAVal | - |
? | |
| L-threonyl-tRNAVal | substrate bound to the enzyme, intermediate in the posttransfer editing reaction | Escherichia coli | L-threonine + tRNAVal | - |
ir | |
| L-threonyl-tRNAVal-AMP | substrate bound to the enzyme, intermediate in the pretransfer editing reaction | Escherichia coli | L-threonine + tRNAVal + AMP | - |
ir | |
| additional information | substrate specificity with diverse Escherichia coli tRNAs and tRNA mutants in editing and aminoacylation reaction, overview | Escherichia coli | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| G7a | - |
Escherichia coli |
| Synthetase, valyl-transfer ribonucleate | - |
Escherichia coli |
| Valine transfer ribonucleate ligase | - |
Escherichia coli |
| Valine translase | - |
Escherichia coli |
| Valine--tRNA ligase | - |
Escherichia coli |
| ValRS | - |
Escherichia coli |
| Valyl transfer ribonucleic acid synthetase | - |
Escherichia coli |
| Valyl-transfer ribonucleate synthetase | - |
Escherichia coli |
| Valyl-transfer RNA synthetase | - |
Escherichia coli |
| Valyl-tRNA ligase | - |
Escherichia coli |
| Valyl-tRNA synthetase | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Escherichia coli | |
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Release 2023.1 (January 2023)
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