Cloned (Comment) | Organism |
---|---|
truncated enzyme lacking 70 amino acid residues in the N-terminus, overexpression in Escherichia coli | Saccharomyces cerevisiae |
Crystallization (Comment) | Organism |
---|---|
purified recombinant truncated enzyme, tri- and tetragonal crystals, X-ry structure determination at 3 and 2.3 A resolution, respectively, molecular replacement, structure analysis and modeling | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-aspartate + tRNAAsp | Saccharomyces cerevisiae | - |
AMP + diphosphate + L-aspartyl-tRNAAsp | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P04802 | dimeric class II aspartyl-tRNA synthetase | - |
Purification (Comment) | Organism |
---|---|
recombinant truncated enzyme from Escherichia coli | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-aspartate + tRNAAsp | - |
Saccharomyces cerevisiae | AMP + diphosphate + L-aspartyl-tRNAAsp | - |
? | |
ATP + L-aspartate + tRNAAsp | tRNA undergoes large conformational changes upon binding to the enzyme, specific charging of amino acid resdiue on tRNA, accurate recognition by the enzyme is achieved through sequence and structural signalling | Saccharomyces cerevisiae | AMP + diphosphate + L-aspartyl-tRNAAsp | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Aspartic acid translase | - |
Saccharomyces cerevisiae |
Aspartyl ribonucleate synthetase | - |
Saccharomyces cerevisiae |
aspartyl ribonuleic synthetase | - |
Saccharomyces cerevisiae |
Aspartyl-transfer ribonucleic acid synthetase | - |
Saccharomyces cerevisiae |
Aspartyl-transfer RNA synthetase | - |
Saccharomyces cerevisiae |
Aspartyl-tRNA synthetase | - |
Saccharomyces cerevisiae |
AspRS | - |
Saccharomyces cerevisiae |