EC Number   |
Protein Variants |
Reference |
|---|
    6.1.1.1 | A74G |
site-directed mutagenesis, replacement of Ala74 with Gly increases the Km 7fold and has no effect on kcat for Tyr. The kcat/Km for Phe decreases 5fold |
745300 |
| 6.1.1.1 | AMSSS |
TyrRS mutant, a library of more than 200 mutants substituting the ATP binding motif KMSSS is built |
704355 |
| 6.1.1.1 | C35G |
crystal structure of mutants Cys to Gly35 and Tyr to Phe34 |
18 |
| 6.1.1.1 | D122N |
site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme |
745300 |
| 6.1.1.1 | D172H |
mutant enzyme shows a significant reductions in tyrosylation activity |
-, 727796 |
| 6.1.1.1 | D172N |
mutant enzyme shows a significant reductions in tyrosylation activity |
-, 727796 |
| 6.1.1.1 | D172P |
mutant enzyme shows a significant reductions in tyrosylation activity |
727796 |
| 6.1.1.1 | D172P |
the mutation completely abolishes tyrosylation activity |
727796 |
| 6.1.1.1 | D194A |
site-directed mutagenesis, mutation does not affect the initial binding of the tRNATyr substrate, it does not destabilize the transition state complex for the second reaction step |
652832 |
| 6.1.1.1 | D286R |
the mutant enzyme aminoacylates the amber suppressor tRNA, as well as the wild-type tRNATyr, whereas the wild-type enzyme aminoacylates the amber suppresssor tRNA about 300fold less efficientyl than the wild-type tRNATyr. The mutant recognizes the amber suppressor tRNA 65fold better than the wild-type enzyme. The activity if the mutant and amber suppressor tRNA pair is as high as 22% that of the wild-type pair. The mutation mainly decreases the KM for tRNA. The kcat is not affected as much |
-, 728359 |
