Application | Comment | Organism |
---|---|---|
molecular biology | the unique widespread distribution of the free-standing editing domain homolog AlaXp is most probably due to singular difficulties, for translation, poised by alanine | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
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 | Escherichia coli |
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 | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-alanine + tRNAAla | - |
Escherichia coli | AMP + diphosphate + L-alanyl-tRNAAla | - |
? |
Synonyms | Comment | Organism |
---|---|---|
alanyl-tRNA synthase | - |
Escherichia coli |
AlaRS | - |
Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Escherichia coli |