EC Number |
Reaction |
Reference |
---|
6.1.1.6 | ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys |
- |
- |
6.1.1.6 | ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys |
active site structure |
652528 |
6.1.1.6 | ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys |
active site structure and substrate binding |
649930 |
6.1.1.6 | ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys |
bases N73, U35 and U36 play an important role in tRNA substrate recognition |
653644 |
6.1.1.6 | ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys |
mechanism of tRNALys and L-lysine binding |
653323 |
6.1.1.6 | ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys |
residue Glu411 plays a key role in the arrangement of diphosphate for the nucleophilic attack |
704351 |
6.1.1.6 | ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys |
sequential ordered mechanism |
-, 479, 501 |
6.1.1.6 | ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys |
Trp314 is involved in binding of L-lysine, binding renders the non-polar microenvironment of the residue more polar |
652901 |
6.1.1.6 | ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys |
two-step binding mechanism |
651752 |
6.1.1.6 | ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys |
two-step reaction mechanism |
649906 |