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Literature summary for 6.1.1.9 extracted from

  • Dulic, M.; Cvetesic, N.; Perona, J.J.; Gruic-Sovulj, I.
    Partitioning of tRNA-dependent editing between pre- and post-transfer pathways in class I aminoacyl-tRNA synthetases (2010), J. Biol. Chem., 285, 23799-23809.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.9

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of His-tagged ValRS in Escherichia coli strain BL21(DE3) Escherichia coli

Protein Variants

Protein Variants Comment Organism
D286A site-directed mutagenesis, the ValRS CP1 domain mutant is unable to deacylate misacylated tRNA even at high enzyme concentrations Escherichia coli
K277P site-directed mutagenesis, the ValRS CP1 domain mutant is unable to deacylate misacylated tRNA even at high enzyme concentrations Escherichia coli
K277P/D286A site-directed mutagenesis, the ValRS CP1 domain mutant is unable to deacylate misacylated tRNA even at high enzyme concentrations Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state parameters for tRNA-independent pre-transfer editing by ValRS and its mutants determined by varying concentrations of noncognate threonine, overview Escherichia coli
5.8
-
 ATP pH 7.5, 37°C, mutant D286A, in presence of tRNA Escherichia coli
9.4
-
 ATP pH 7.5, 37°C, wild-type ValRS, in presence of tRNA Escherichia coli
10.7
-
 ATP pH 7.5, 37°C, mutant K277P/D286A, in presence of tRNA Escherichia coli
13.4
-
 ATP pH 7.5, 37°C, mutant K277P, in presence of tRNA Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ assay at Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged ValRS from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 in ValRS transfer to tRNA is 200fold faster than hydrolysis Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-valine + tRNAVal
-
 Escherichia coli AMP + diphosphate + L-valyl-tRNAVal
-
 ?

Synonyms

Synonyms Comment Organism
More the enzyme is a class I aminoacyl-tRNA synthetase Escherichia coli
ValRS
-
 Escherichia coli
Valyl-tRNA synthetase
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at, aminoacylation and deacylation reactions Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.28
-
 ATP pH 7.5, 37°C, mutant D286A, in presence of tRNA Escherichia coli
0.34
-
 ATP pH 7.5, 37°C, mutant K277P, in presence of tRNA Escherichia coli
0.48
-
 ATP pH 7.5, 37°C, mutant K277P/D286A, in presence of tRNA Escherichia coli
12.9
-
 ATP pH 7.5, 37°C, wild-type ValRS, in presence of tRNA Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at, aminoacylation and deacylation reactions Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function hydrolytic editing activities are present in aminoacyl-tRNA synthetases possessing reduced amino acid discrimination in the synthetic reactions. Post-transfer hydrolysis of misacylated tRNA in class I editing enzymes, e.g. ValRS, occurs in a spatially separate domain inserted into the catalytic Rossmann fold, location and mechanisms of pre-transfer hydrolysis of misactivated amino acids, overview. The rates of amino acid transfer to tRNA are similar for cognate and noncognate aminoacyl-adenylates. Editing by ValRS occurs nearly exclusively by post-transfer hydrolysis in the editing domain Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.03
-
 ATP pH 7.5, 37°C, mutant K277P, in presence of tRNA Escherichia coli
0.05
-
 ATP pH 7.5, 37°C, mutant D286A, in presence of tRNA Escherichia coli
0.05
-
 ATP pH 7.5, 37°C, mutant K277P/D286A, in presence of tRNA Escherichia coli
1.37
-
 ATP pH 7.5, 37°C, wild-type ValRS, in presence of tRNA Escherichia coli