EC Number | Crystallization (Comment) | Organism |
---|---|---|
6.1.1.23 | purified 520 kDa transamidosome complex formed by two dimeric nondiscriminating-AspRSs, two trimeric GatCABs, and four tRNAsAsn molecules, X-ray diffraction structure determination and analysis at 3.0 A resolution, molecular replacement | Thermus thermophilus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.1.1.23 | additional information | - |
additional information | pre-steady-state and steady-state aminoacylation kinetics of the ND-AspRSK-tRNAAsn complex and of the transamidosome, overview | Thermus thermophilus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.1.1.23 | Mg2+ | required | Thermus thermophilus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.1.1.23 | ATP + L-aspartate + tRNAAsn | Thermus thermophilus | - |
AMP + diphosphate + L-aspartyl-tRNAAsn | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.1.1.23 | Thermus thermophilus | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.1.1.23 | ATP + L-aspartate + tRNAAsn | - |
Thermus thermophilus | AMP + diphosphate + L-aspartyl-tRNAAsn | - |
? | |
6.1.1.23 | ATP + L-aspartate + tRNAAsn | ND-AspRSKtRNAAsn complex and of the transamidosome and mechanism of transamidation, overview. A scaffold tRNAAsn mediates stability and integrity of the complex | Thermus thermophilus | AMP + diphosphate + L-aspartyl-tRNAAsn | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
6.1.1.23 | More | comparison of three-dimensional transamidosome complex structures in crystals and in solution, overview | Thermus thermophilus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.1.1.23 | non-discriminating aspartyl-tRNA synthetase | - |
Thermus thermophilus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
6.1.1.23 | 25 | - |
assay at | Thermus thermophilus |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
6.1.1.23 | 10 | 85 | transamidosome complex: ND-AspRS is thermostable up to 70°C, but its thermostability increases when complexed to tRNAAsn. tRNAAsn is very stable, as its melting temperature is 85°C. the GatCAB is poorly protected against heat inactivation, as its denaturation starts at 40°C, but when complexed in the transamidosome, the GatCAB becomes fully thermostable at 85°C | Thermus thermophilus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
6.1.1.23 | 7.2 | - |
assay at | Thermus thermophilus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.1.1.23 | ATP | - |
Thermus thermophilus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
6.1.1.23 | physiological function | during tRNA-dependent asparagine formation, tRNAAsn promotes assembly of a ribonucleoprotein particle called transamidosome that allows channelling of the aa-tRNA from non-discriminating aspartyl-tRNA synthetase active site to the GatCAB amidotransferase site. A transamidosome particle is formed by two GatCABs, two dimeric nondiscriminating-AspRSs and four tRNAsAsn molecules. In the complex, only two tRNAs are bound in a functional state, whereas the two other ones act as an RNA scaffold enabling release of the asparaginyl-tRNAAsn without dissociation of the complex. The transamidosome constitutes a transfer-ribonucleoprotein particle in which tRNAs serve the function of both substrate and structural foundation for a large molecular machine | Thermus thermophilus |