Any feedback?
Literature summary for 6.1.1.12 extracted from
- Expression of human aspartyl-tRNA synthetase in Escherichia coli. Functional analysis of the N-terminal putative amphiphilic helix (1993), J. Biol. Chem., 268, 6014-6023.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| wild-type enzyme and N-terminal 32-residues truncated form, expressed in Escherichia coli as fusion proteins linked through a thrombin cleavage site with glutathione-S-transferase | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| hDRSDELTA32 | N-terminal 32-residue truncated form, hDRSDELTA32, with lower thermal stability and ATP-diphosphate exchange activity, but higher aminoacylation activity. Fusion protein of glutathione-S-transferase and hDRSDELTA32 with lower thermal stability | Homo sapiens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.000013 | - |
tRNAAsp | native enzyme | Homo sapiens |  |
| 0.00013 | - |
tRNAAsp | truncated enzyme | Homo sapiens | |
| 0.029 | - |
Asp | truncated enzyme | Homo sapiens | |
| 0.302 | - |
Asp | native enzyme | Homo sapiens | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacteria | - |
- |
- |
| Homo sapiens | - |
wild-type and N-terminal 32-residue truncated form (hDRS delta 32) expressed in Escherichia coli | - |
| Mammalia | - |
- |
- |
| Saccharomyces cerevisiae | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| wild-type enzyme and N-terminal 32-residue truncated form (hDRS delta 32), expressed in Escherichia coli as fusion proteins linked through a thrombin cleavage site with glutathione-S-transferase | Homo sapiens |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.017 | - |
wild-type enzyme | Homo sapiens |
| 0.034 | - |
truncated enzyme | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-aspartate + tRNAAsp | - |
Mammalia | AMP + diphosphate + L-aspartyl-tRNAAsp | - |
? | |
| ATP + L-aspartate + tRNAAsp | - |
Bacteria | AMP + diphosphate + L-aspartyl-tRNAAsp | - |
? | |
| ATP + L-aspartate + tRNAAsp | - |
Homo sapiens | AMP + diphosphate + L-aspartyl-tRNAAsp | - |
? | |
| ATP + L-aspartate + tRNAAsp | - |
Saccharomyces cerevisiae | AMP + diphosphate + L-aspartyl-tRNAAsp | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | enzyme occurs in the multienzyme complex of aminoacyl-tRNA synthetases | Mammalia |
| More | enzymes exist as free soluble enzymes | Bacteria |
| More | enzymes exist as free soluble enzymes | Saccharomyces cerevisiae |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
native enzyme is stable for 24 h, half-life of truncated enzyme hDRSDELTA32 is 7 h, half-life of the fusion protein of glutathione-S-transferase and hDRSDELTA32 is 3 h | Homo sapiens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
