EC Number   |
Natural Substrates |
|---|
    6.1.1.20 | ATP + 4-azido-L-phenylalanine + tRNAPhe |
- |
| 6.1.1.20 | ATP + L-phenylalanine + tRNAPhe |
- |
| 6.1.1.20 | ATP + L-phenylalanine + tRNAPhe |
enzyme is essemtial for poly(Phe) synthesis |
| 6.1.1.20 | ATP + L-phenylalanine + tRNAPhe |
cognate amino acid charging |
| 6.1.1.20 | ATP + L-phenylalanine + tRNAPhe |
the enzyme is responsible for synthesizing Phe-tRNAPhe during protein synthesis |
| 6.1.1.20 | ATP + L-tyrosine + tRNAPhe |
PheRS misactivates Tyr but is able to correct the mistake using a proofreading editing activity, overview, after evading editing by PheRS, Tyr-tRNAPhe is recognized by elongation factor Tu EF-Tu, involved in translational quality control including substrate selection by aminoacyl-tRNA synthetases, as efficiently as the cognate Phe-tRNAPhe, overview |
| 6.1.1.20 | more |
enzyme expression, genes pheS and pheT, is regulated by iron availability |
| 6.1.1.20 | more |
phylogenetic analysis |
| 6.1.1.20 | more |
the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA |
| 6.1.1.20 | more |
the enzyme might by its DNA binding capacity be involved in cellular processes of cell proliferation |
