EC Number |
Reaction |
Reference |
---|
6.1.1.12 | ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp |
- |
- |
6.1.1.12 | ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp |
active site residues |
650960 |
6.1.1.12 | ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp |
active site structure |
652818 |
6.1.1.12 | ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp |
active site structure, AspRS substrate recognition and chiral specificity of wild-type enzyme and mutant Q199E, substrate binding in regular versus inverted orientation, overview |
674863 |
6.1.1.12 | ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp |
active site structure, ligand and substrate binding, and reaction mechanism |
674621 |
6.1.1.12 | ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp |
Asn binding sites K198 and H449, binding mechanism and free energies |
652847 |
6.1.1.12 | ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp |
conserved amino acid residues of functional importance in consensus motifs: Pro227 in motif 1, Arg332 and Glu334 in motif 2, Gly675, Gly679, Asp681, Arg682, and Pro700 in motif 3 |
-, 440089 |
6.1.1.12 | ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp |
conserved amino acid residues of functional importance in consensus motifs: Pro227 in motif 1, Arg332 and Glu334 in motif 2, Gly675, Gly679, Glu681, Arg682, and Pro700 in motif 3 |
-, 440089 |
6.1.1.12 | ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp |
determination of structural features for discriminating or nondiscriminating aminoacylation activity |
650996 |
6.1.1.12 | ATP + L-aspartate + tRNAAsp = AMP + diphosphate + L-aspartyl-tRNAAsp |
mechanism |
652801 |