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Literature summary for 6.1.1.7 extracted from

  • Pasman, Z.; Robey-Bond, S.; Mirando, A.C.; Smith, G.J.; Lague, A.; Francklyn, C.S.
    Substrate specificity and catalysis by the editing active site of alanyl-tRNA synthetase from Escherichia coli (2011), Biochemistry, 50, 1474-1482.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.7

Protein Variants

Protein Variants Comment Organism
C666A site-directed mutagenesis, the mutant shows reduced deacylation rates of tRNAAla compared to the wild-type enzyme Escherichia coli
E664A site-directed mutagenesis, the mutant shows reduced deacylation rates of tRNAAla compared to the wild-type enzyme Escherichia coli
I667E site-directed mutagenesis, the mutant shows reduced deacylation rates of tRNAAla compared to the wild-type enzyme Escherichia coli
additional information mutagenesis of the AlaRS editing active site Escherichia coli
Q584N site-directed mutagenesis, the mutant shows reduced deacylation rates of tRNAAla compared to the wild-type enzyme Escherichia coli
T567G site-directed mutagenesis, the mutant shows reduced deacylation rates of tRNAAla compared to the wild-type enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state kinetic parameters for deacylation of aa-tRNAAla at 37°C and pH 7.5 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli
Zn2+ potential role of the coordinated zinc in editing substrate specificity Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli analysis of the deacylation activities of the wild type and five different Escherichia coli AlaRS editing site substitution mutants using the free-standing Pyrococcus horikoshii AlaX editing domain complexed with serine as a model and both Ser-tRNAAla and Ala-tRNAAla as substrates, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information analysis of the deacylation activities of the wild type and five different Escherichia coli AlaRS editing site substitution mutants using the free-standing Pyrococcus horikoshii AlaX editing domain complexed with serine as a model and both Ser-tRNAAla and Ala-tRNAAla as substrates, overview Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
Alanyl-tRNA synthetase
-
 Escherichia coli
AlaRS
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at, deacylation assay with aminoacylated tRNAAla as substrate Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at, deacylation assay with aminoacylated tRNAAla as substrate Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function the relatively modest specificity of the AlaRS editing domain may provide a rationale for the widespread phylogenetic distribution of AlaX free-standing editing domains, thereby contributing a further mechanism to lower concentrations of misacylated tRNAAla Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
additional information
-
 additional information the wild-type AlaRS editing domain deacylates Ser-tRNAAla with a kcat/Km of 66 mM/s, equivalent to a rate enhancement of 6000 over the rate of enzyme-independent deacylation but only 12.2fold greater than the rate with Ala-tRNAAla. While the E664A and T567G substitutions only minimally decrease kcat/Km, Q584H, I667E, and C666A AlaRS are more compromised in activity, with decreases in kcat/Km in the range of 6fold, 6.6fold, and 15fold. C666A AlaRS is 1.7fold more active on Ala-tRNAAla relative to Ser-tRNAAl. Deacylation rates of Ser-tRNAAla and Ala-tRNAAla in the absence of enzyme are determined by fitting the progress curves to equations describing a first-order decay Escherichia coli