EC Number |
Reaction |
Reference |
---|
6.1.1.9 | ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal |
- |
- |
6.1.1.9 | ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal |
Lys593 and Lys554 are in the active site binding valine or threonine, part of the 554KMSKS558 consensus sequence, mechanism, determination of diverse amino acid residues of the enzyme molecule involved in substrate binding, Lys277 plays a crucial role in the fidelity of tRNA aminoacylation by the enzyme, nucleophilic attack of misacylated tRNA in the diting site of the enzyme |
650122 |
6.1.1.9 | ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal |
mechanism and structural basis of molecular interactions of the enzyme with the C34A35C36 anticodon for tRNAVal recognition by the enzyme |
653871 |
6.1.1.9 | ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal |
pre- and post-transfer editing mechanism, mechanism, active site/editing site |
650777 |
6.1.1.9 | ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal |
substrate binding mechanism, bases A73 and C75 are involved in the tRNA substrate recognition and editing reaction |
653390 |
6.1.1.9 | ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal |
tRNAVal 3'-end, and a purine at position 76, is crucial for substrate editing mechanism |
650085 |