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Literature summary for 6.1.1.4 extracted from
- The peptide bond between E292-A293 of Escherichia coli leucyl-tRNA synthetase is essential for its activity (1999), Biochemistry, 38, 13063-13069.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression and assembly of the 63 and 34 kDa peptides in Escherichia coli strain KL231 cannot complement the deficient temperature-sensitive strain, while expression of peptide fragments derived by cleavage of other peptide bonds leads to assembly of a functional enzyme | Escherichia coli |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 34000 | - |
x * 34000, N-terminal peptide after cleavage of peptide bond E292-A293, SDS-PAGE, x * 63000, C-terminal peptide after cleavage of peptide bond E292-A293, SDS-PAGE, x * 97300, recombinant wild-type enzyme, SDS-PAGE | Escherichia coli |
| 63000 | - |
x * 34000, N-terminal peptide after cleavage of peptide bond E292-A293, SDS-PAGE, x * 63000, C-terminal peptide after cleavage of peptide bond E292-A293, SDS-PAGE, x * 97300, recombinant wild-type enzyme, SDS-PAGE | Escherichia coli |
| 97300 | - |
x * 34000, N-terminal peptide after cleavage of peptide bond E292-A293, SDS-PAGE, x * 63000, C-terminal peptide after cleavage of peptide bond E292-A293, SDS-PAGE, x * 97300, recombinant wild-type enzyme, SDS-PAGE | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-leucine + tRNALeu | Escherichia coli | - |
AMP + diphosphate + L-leucyl-tRNALeu | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
class I enzyme | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| additional information | the enzyme contains proteolytic cleavage sites at the peptide bonds between T252 and F253, E292 and A293, K327 and A328, and P368 and D369 | Escherichia coli |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type enzyme from overexpression in Escherichia coli, purification of the proteolytically derived fragments from wild-type enzyme preparation | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 2.8 | - |
purified recombinant enzyme | Escherichia coli |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -20°C, 10 mg/ml of enzyme, 1 month, partial cleavage of the enzyme into peptides of 63 and 34 kDA occurs, loss of 30% aminoacylation activity | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-leucine + tRNALeu | - |
Escherichia coli | AMP + diphosphate + L-leucyl-tRNALeu | - |
? | |
| ATP + L-leucine + tRNALeu | the peptide bond between Glu292 and Ala293 in the large connecting polypeptide CP1 is essential for activity | Escherichia coli | AMP + diphosphate + L-leucyl-tRNALeu | - |
? | |
| additional information | proteolytically derived 34 kDa peptide fragment has lost most of its aminoacylation activity, but retains the ATP-dihosphate exchnage activity, the enzyme also performs the ATP-diphosphate exchange reaction | Escherichia coli | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 34000, N-terminal peptide after cleavage of peptide bond E292-A293, SDS-PAGE, x * 63000, C-terminal peptide after cleavage of peptide bond E292-A293, SDS-PAGE, x * 97300, recombinant wild-type enzyme, SDS-PAGE | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Leucine translase | - |
Escherichia coli |
| Leucine--tRNA ligase | - |
Escherichia coli |
| Leucyl-transfer ribonucleate synthetase | - |
Escherichia coli |
| Leucyl-transfer ribonucleic acid synthetase | - |
Escherichia coli |
| Leucyl-transfer RNA synthetase | - |
Escherichia coli |
| Leucyl-tRNA synthetase | - |
Escherichia coli |
| LeuRS | - |
Escherichia coli |
| Synthetase, leucyl-transfer ribonucleate | - |
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 |
|---|---|---|---|
| 7.8 | - |
ATP-diphosphate exchange assay at | Escherichia coli |
| 8 | - |
aminoacylation assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Escherichia coli | |
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