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Literature summary for 6.1.1.9 extracted from

  • Tardif, K.D.; Liu, M.; Vitseva, O.; Hou, Y.M.; Horowitz, J.
    Misacylation and editing by Escherichia coli valyl-tRNA synthetase: evidence for two tRNA binding sites (2001), Biochemistry, 40, 8118-8125.
    View publication on PubMed
Search for more literature for 6.1.1.9

Inhibitors

Inhibitors Comment Organism Structure
Thr-tRNAValC76
-
 Escherichia coli
tRNAVal(-ACCA)
-
 Escherichia coli
tRNAVal(-CCA)
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0395
-
 L-valine pH 7.5, 37°C Escherichia coli
1.9
-
 L-isoleucine pH 7.5, 37°C Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal tRNAVal 3'-end, and a purine at position 76, is crucial for substrate editing mechanism Escherichia coli
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-isoleucine + tRNAVal very low activity Escherichia coli AMP + diphosphate + L-isoleucyl-tRNAVal
-
 ?
ATP + L-valine + tRNAVal
-
 Escherichia coli AMP + diphosphate + L-valyl-tRNAVal
-
 ?
ATP + L-valine + tRNAVal enzyme contains 2 tRNA binding sites involved in aminoacetylation and editing reactions, misacetylated tRNAVal is edited by the enzyme to avoid accumulation, the 3'-end of the tRNA is involved Escherichia coli AMP + diphosphate + L-valyl-tRNAVal
-
 ?
additional information tRNAVal variants in position 76, i.e. U76, C76, G76 activate the editing activity, misactivation of threonine, alanine, serine, cysteine, alpha-aminobutyrate, and to a low extent of norvaline activates the editing reaction at different rates, overview, the enzyme is unable to deacylate misacylated tRNAVal terminating in 3'-pyrimidines but does deacylate mischarged tRNAVal terminating in adenosine or guanosine, no misactivation of methionine, leucine, glycine, glutamic acid, lysine, tyrosine, and phenylalanine Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
G7a
-
 Escherichia coli
Synthetase, valyl-transfer ribonucleate
-
 Escherichia coli
Valine transfer ribonucleate ligase
-
 Escherichia coli
Valine translase
-
 Escherichia coli
Valine--tRNA ligase
-
 Escherichia coli
ValRS
-
 Escherichia coli
Valyl transfer ribonucleic acid synthetase
-
 Escherichia coli
Valyl-transfer ribonucleate synthetase
-
 Escherichia coli
Valyl-transfer RNA synthetase
-
 Escherichia coli
Valyl-tRNA ligase
-
 Escherichia coli
Valyl-tRNA synthetase
-
 Escherichia coli

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information inhibition kinetics Escherichia coli
0.0085
-
 Thr-tRNAValC76
-
 Escherichia coli
0.02
-
 tRNAVal(-ACCA) pH 7.5, 37°C Escherichia coli
0.029
-
 tRNAVal(-CCA) pH 7.5, 37°C Escherichia coli