EC Number |
Protein Variants |
Reference |
---|
6.1.1.7 | A77V |
naturally occuring mutation of a catalytic residue. the mutant likely affects alanine binding resulting in either totally inactive enzyme or with little aminoacylation activity due to decreased affinity to alanine |
744969 |
6.1.1.7 | C290S |
mutant enzymes with replacement of Cys residues, Cys76Ser, Cys290Ser, Cys412Ser, Cys665Ser. Mutation of Cys665 to serine induces a 120-fold decrease in catalytic efficiency |
515 |
6.1.1.7 | C665S |
mutant enzymes with replacement of Cys residues, Cys76Ser, Cys290Ser, Cys412Ser, Cys665Ser. Mutation of Cys665 to serine induces a 120-fold decrease in catalytic efficiency |
515 |
6.1.1.7 | C666A |
site-directed mutagenesis, the mutant shows reduced deacylation rates of tRNAAla compared to the wild-type enzyme |
714234 |
6.1.1.7 | C666A/Q584H |
aminoacylation activity is unchanged from that of wild-type. In contrast to the wild-type protein mutant protein mischarges Ser onto tRNAAla. Consistent with this mischarging, deacylation of Ser-tRNA Ala by the mutant protein is undetecable. Mutant protein is sensitive to high concentrations of serine |
693161 |
6.1.1.7 | C666A/Q584H |
Serine toxicity, experienced by a strain harboring an C666A/Q584H editing-defective alanyl-tRNA synthetase mutant, is rescued by an AlaXp-encoding transgene from Methanosarcina mazei. AlaXp is a free-standing editing domain homolog of AlaRS. Rescue is dependent on amino acid residues in AlaXp that are needed for its in vitro catalytic activity |
693161 |
6.1.1.7 | C76S |
mutant enzymes with replacement of Cys residues, Cys76Ser, Cys290Ser, Cys412Ser, Cys665Ser. Mutation of Cys665 to serine induces a 120-fold decrease in catalytic efficiency |
515 |
6.1.1.7 | D235A |
no improvement in the discrimination between alanine and serine |
705890 |
6.1.1.7 | D235E |
no improvement in the discrimination between alanine and serine |
705890 |
6.1.1.7 | D235N |
no improvement in the discrimination between alanine and serine |
705890 |