Protein Variants | Comment | Organism |
---|---|---|
additional information | the deletion mutant lacking the C-terminal domain, LeuRSDELTA811-967, retains normal editing activity, but has severely reduced aminoacylation activity, deletion of amino acid residues 911-913 of LeuRS enhances the Ile-tRNAIle deacylation activity, without affecting the Ile-tRNALeu deacylation activity, a C-terminally truncated LeuRS can catalyze the first step of the aminoacylation reaction, Leu-AMP formation, but cannot catalyze the second step, transfer of Leu from Leu-AMP to tRNALeu, overview | Pyrococcus horikoshii |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00167 | - |
tRNALeu | full-length enzyme, pH 7.5, 37°C | Pyrococcus horikoshii | |
0.00179 | - |
tRNALeu | truncation mutant DELTA911-913, pH 7.5, 37°C | Pyrococcus horikoshii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Pyrococcus horikoshii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-leucine + tRNALeu | Pyrococcus horikoshii | - |
AMP + diphosphate + L-leucyl-tRNALeu | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus horikoshii | - |
- |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
activity and specificity of several truncation and deletion mutants, overview | Pyrococcus horikoshii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-leucine + tRNALeu | - |
Pyrococcus horikoshii | AMP + diphosphate + L-leucyl-tRNALeu | - |
? | |
ATP + L-leucine + tRNALeu | a two step reaction, the C-terminal domain recognizes the long variable arm of tRNALeu for aminoacylation, and the so-called editing domain deacylates incorrectly formed Ile-tRNALeu, structural superposition of tRNAIle onto the LeuRS-tRNALeu complex indicated that Ile911, Lys912, and Glu913 of the LeuRS C-terminal domain clash with U20 of tRNAIle, which is bulged out as compared to the corresponding nucleotide of tRNALeu, mechanism for prevention of misediting, overview | Pyrococcus horikoshii | AMP + diphosphate + L-leucyl-tRNALeu | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | enzyme structure and tRNA binding site, the requirement of the C-terminal domain for misediting prevention is unique to LeuR, overview | Pyrococcus horikoshii |
Synonyms | Comment | Organism |
---|---|---|
Leucyl-tRNA synthetase | - |
Pyrococcus horikoshii |
LeuRS | - |
Pyrococcus horikoshii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Pyrococcus horikoshii |
65 | - |
misformation assay at | Pyrococcus horikoshii |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | 65 | - |
Pyrococcus horikoshii |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.177 | - |
tRNALeu | truncation mutant DELTA911-913, pH 7.5, 37°C | Pyrococcus horikoshii | |
0.331 | - |
tRNALeu | full-length enzyme, pH 7.5, 37°C | Pyrococcus horikoshii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Pyrococcus horikoshii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Pyrococcus horikoshii |