Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Thermus thermophilus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-leucine + tRNALeu | Thermus thermophilus | - |
AMP + diphosphate + L-leucyl-tRNALeu | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermus thermophilus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-leucine + tRNALeu | - |
Thermus thermophilus | AMP + diphosphate + L-leucyl-tRNALeu | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Leucyl-tRNA synthetase | - |
Thermus thermophilus |
LeuRS | - |
Thermus thermophilus |
More | the enzyme belongs to the class I aminoacyl-tRNA synthetases | Thermus thermophilus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Thermus thermophilus |
General Information | Comment | Organism |
---|---|---|
physiological function | aminoacyl-tRNA synthetases are critical for the translational process, catalyzing the attachment of specific amino acids to their cognate tRNAs. To ensure formation of the correct aminoacyl-tRNA, and thereby enhance the reliability of translation, several aminoacyl-tRNA synthetases have an editing capability that hinders formation of misaminoacylated tRNAs, analysis of the mechanism of the editing reaction for class I enzyme leucyl-tRNA synthetase complexed with a misaminoacylated tRNALeu by initio hybrid quantum mechanical/molecular mechanical potentials in conjunction with molecular dynamics simulations, overview. Editing is a self-cleavage reaction of the tRNA and so it is the tRNA, and not the protein, that drives the reaction. The protein does, however, have an important stabilizing effect on some high-energy intermediates along the reaction path, which is more efficient than the ribozyme would be alone. This indicates that editing is achieved by a hybrid ribozyme/protein catalyst. The water molecule that acts as the nucleophile in the editing reaction is activated by a 3'-hydroxyl group at the 3'-end of tRNALeu and that the O2' atom of the leaving group of the substrate is capped by one of the water's hydrogen atoms | Thermus thermophilus |