EC Number   |
Protein Variants |
Reference |
|---|
    6.1.1.24 | E334R/G417T/ |
mutant of GluRS2 specifically and more robustly aminoacylates tRNAGlu1 instead of tRNAGln |
-, 659722 |
| 6.1.1.24 | G417T |
mutant GluRS2 shows weak activity towards tRNAGlu1 |
-, 659722 |
| 6.1.1.24 | L1L2 |
site-directed mutagenesis, construction of a hybrid enzyme, kinetic comparison to wild-type enzyme and other hybrid enzyme mutants |
714207 |
| 6.1.1.24 | more |
construction of a hybrid enzyme in which 23 amino acids from the catalytic domain of Escherichia coli glutaminyl-tRNA synthetase, GlnRS, are replaced with the corresponding residues of human glutamyl-tRNA synthetase, GluRS. Further introduction of two distal surface loops bridging core secondary structural elements of the Rossmann fold then produces a hybrid enzyme GlnRS S1/L1/L2. The engineered hybrid GlnRS S1/L1/L2 synthesizes Glu-tRNAGln over 104fold more efficiently than GlnRS, overview. The simultaneous optimization of paired amino acid and tRNA binding sites found in a naturally occurring enzyme is not recapitulated in a hybrid that is successfully engineered for amino acid complementarity. Design and characterization of four additional hybrids identify further residues involved in improving complementarity for glutamate and in communicating between amino acid and tRNA binding sites, complementarity for tRNA, mutant enzyme structure, overview. Relationship between tRNA and amino acid binding sites in the hybrid enzymes, overview |
714207 |
| 6.1.1.24 | more |
the engineered mutant hybrid C229R Gln-RS, EC 6.1.1.18, shows activity with L-glutamine or L-glutamate and tRNAGln like the nondiscriminating enzyme, EC 6.1.1.24. Introduction of 22 amino acid replacements and one deletion, including substitution of the entire primary binding site and two surface loops adjacent to the region disrupted in the mutant C229R, improves the capacity of the mutant enzyme to synthesize misacylated Glu-tRNAGln by 16000fold, overview |
694903 |
| 6.1.1.24 | T231L |
site-directed mutagenesis, construction of a hybrid enzyme, kinetic comparison to wild-type enzyme and other hybrid enzyme mutants |
714207 |
| 6.1.1.24 | V218S |
site-directed mutagenesis, construction of a hybrid enzyme, kinetic comparison to wild-type enzyme and other hybrid enzyme mutants |
714207 |
| 6.1.1.24 | W256Y |
site-directed mutagenesis, construction of a hybrid enzyme, kinetic comparison to wild-type enzyme and other hybrid enzyme mutants |
714207 |
| 6.1.1.24 | Y240D/D241F |
site-directed mutagenesis, construction of a hybrid enzyme, kinetic comparison to wild-type enzyme and other hybrid enzyme mutants |
714207 |
