EC Number   |
Protein Variants |
Reference |
|---|
    6.1.1.6 | A233S |
the mutant recognizes L-lysine better than wild type and shows higher catalytic efficiency |
727514 |
| 6.1.1.6 | A233S/G469A |
inactive, the mutation decreases stable L-lysyl-adenylate formation |
727514 |
| 6.1.1.6 | CAT W314F |
mutant of the truncated C-terminal catalytic domain CAT |
691093 |
| 6.1.1.6 | CAT W332F |
mutant of the truncated C-terminal catalytic domain CAT |
691093 |
| 6.1.1.6 | DELTA1-65 |
mutant enzyme binds poorly to tRNALys, but does not increase tRNALys packaging into HIV-1 viruses |
662735 |
| 6.1.1.6 | DELTA452-597 |
mutant enzyme binds to but does not aminoacylate tRNALys, still facilitates an increase in tRNALys packaging into virions |
662735 |
| 6.1.1.6 | DELTAS70-T584 |
truncation at S70-T584 and full length LysRS (M1-V597) expressed, purified, and attempted for crystallization |
694885 |
| 6.1.1.6 | E240D |
1.2fold increase in Km-value for Lys, 21fold decrease in turnover number for Lys, Km-value for ATP is nearly identical to wild-type value, 24fold decrease in turnover number for ATP |
661087 |
| 6.1.1.6 | E240Q |
1.4fold increase in Km-value for Lys, 207fold decrease in turnover number for Lys, 1.2fold increase in Km-value for ATP, 261fold decrease in turnover number for ATP |
661087 |
| 6.1.1.6 | E246D |
the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme |
727475 |
