EC Number   |
Protein Variants |
Reference |
|---|
    6.1.1.20 | A141W |
site-directed mutagenesis, the mutant exhibits high tyrosine mischarging activity |
676814 |
| 6.1.1.20 | A249G/A356W |
mutant enzyme with A294G mutation in alpha-subunit and A356W mutation in beta-subunit, kcat/Km is 6.6% of wild-type value |
668401 |
| 6.1.1.20 | A249G/E334A |
mutant enzyme with A294G mutation in alpha-subunit and E334A mutation in beta-subunit, kcat/Km is 60% of wild-type value |
668401 |
| 6.1.1.20 | A249G/H265A |
mutant enzyme with A294G mutation in alpha-subunit and H265A mutation in beta-subunit, kcat/Km is 52% of wild-type value |
668401 |
| 6.1.1.20 | A249G/H265L |
mutant enzyme with A294G mutation in alpha-subunit and H265L mutation in beta-subunit, kcat/Km is 63% of wild-type value |
668401 |
| 6.1.1.20 | A249G/T354W |
mutant enzyme with A294G mutation in alpha-subunit and T354W mutation in beta-subunit, kcat/Km is 26% of wild-type value |
668401 |
| 6.1.1.20 | A293X |
p-fluorophenylalanine-resistant strain with Ala294Ser, Ala293X or Ala295X mutation. Phe293 and Phe295 are not directly involved in substrate binding, but replacements of these residues affect PheRS stability. Exchanges at position 294 alter the binding of Phe, and certain mutants show pronounced changes in specificity towards Phe analogues |
325 |
| 6.1.1.20 | A294G |
EcPheRS mutant |
706561 |
| 6.1.1.20 | A294G |
mutant enzyme with A294G mutation in alpha-subunit, kcat/Km is 58% of wild-type value |
668401 |
| 6.1.1.20 | A294G |
mutation of the catalytical alpha-subunit, constructed mutant shows relaxed substrate specificity, efficient incorporation of p-iodo, p-ethynyl-, p-cyano-, and p-azidophenylalanines, but not p-acetylphenylalanine, into protein in the Escherichia coli host |
651585 |
