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Literature summary for 6.1.1.7 extracted from

  • Chong, Y.E.; Yang, X.L.; Schimmel, P.
    Natural homolog of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation (2008), J. Biol. Chem., 283, 30073-30078.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.7

Application

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

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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-alanine + tRNAAla
-
 Escherichia coli AMP + diphosphate + L-alanyl-tRNAAla
-
 ?

Synonyms

Synonyms Comment Organism
alanyl-tRNA synthase
-
 Escherichia coli
AlaRS
-
 Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli