EC Number   |
Reaction |
Reference |
|---|
    6.1.1.3 | ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr |
- |
- |
| 6.1.1.3 | ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr |
active site structure |
653312 |
| 6.1.1.3 | ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr |
bi uni uni bi ping-pong mechanism |
- |
| 6.1.1.3 | ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr |
determination of substrate binding sites, catalytic sites, and catalytic mechanism from structure modeling |
663379 |
| 6.1.1.3 | ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr |
functional mechanism and substrate recognition, editing model, 2 separate active sites for substrate binding, binding of tRNA is more specific than the binding of the amino acid |
650778 |
| 6.1.1.3 | ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr |
induced fit, Trp434 is involved in conformational changes during substrate binding |
650200 |
| 6.1.1.3 | ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr |
mechanism, active site structure, and substrate recognition method |
650784 |
| 6.1.1.3 | ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr |
reaction mechanism analysis by QM/MM and MM modeling of full length and truncated enzyme, molecular mechanism simulation |
663398 |
| 6.1.1.3 | ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr |
reaction mechanism and structure-function relationship, modeling, overview |
743906 |
| 6.1.1.3 | ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr |
reaction mechanism and structure-function relationship, overview. Molecular dynamics simulation study of the dynamics of the active site organization during charging step of dimeric ThrRS from Escherichia coli (ecThrRS) bound with ectRNAThr |
745397 |
