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Literature summary for 6.1.1.6 extracted from

  • Takita, T.; Akita, E.; Inouye, K.; Tonomura, B.i.
    Lysyl-tRNA synthetase from Bacillus stearothermophilus. Stopped-flow kinetic analysis of enzyme.lysyladenylate formation (1998), J. Biochem., 124, 45-50.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics Geobacillus stearothermophilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57700
-
2 * 57700, SDS-PAGE Geobacillus stearothermophilus
115400
-
about Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + lysine + tRNALys Geobacillus stearothermophilus
-
AMP + L-lysyl-tRNALys + diphosphate
-
r

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
NCA1503, purified enzyme
-

Reaction

Reaction Comment Organism Reaction ID
ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys two-step binding mechanism Geobacillus stearothermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-lysine + tRNALys the L-lysine binding process is much faster than the ATP binding process Geobacillus stearothermophilus AMP + L-lysyl-tRNALys + diphosphate
-
r
ATP + L-lysine amide + tRNALys
-
Geobacillus stearothermophilus AMP + L-amino-lysyl-tRNALys + diphosphate
-
r
ATP + L-lysine hydroxamate + tRNALys
-
Geobacillus stearothermophilus AMP + L-lysine hydroxamoyl-tRNALys + diphosphate
-
r
ATP + lysine + tRNALys
-
Geobacillus stearothermophilus AMP + L-lysyl-tRNALys + diphosphate
-
r

Subunits

Subunits Comment Organism
dimer 2 * 57700, SDS-PAGE Geobacillus stearothermophilus

Synonyms

Synonyms Comment Organism
L-Lysine-transfer RNA ligase
-
Geobacillus stearothermophilus
Lysine translase
-
Geobacillus stearothermophilus
Lysine--tRNA ligase
-
Geobacillus stearothermophilus
Lysine-tRNA synthetase
-
Geobacillus stearothermophilus
LysRS
-
Geobacillus stearothermophilus
Lysyl-transfer ribonucleate synthetase
-
Geobacillus stearothermophilus
Lysyl-transfer RNA synthetase
-
Geobacillus stearothermophilus
Lysyl-tRNA synthetase
-
Geobacillus stearothermophilus
Synthetase, lysyl-transfer ribonucleate
-
Geobacillus stearothermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Geobacillus stearothermophilus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information hyperbolic dependence of kapp on the initial ATP concentration Geobacillus stearothermophilus
14.5
-
L-Lysine amide forward reaction, pH 8.0, 30°C Geobacillus stearothermophilus
45.7
-
L-lysine forward reaction, pH 8.0, 30°C Geobacillus stearothermophilus
221
-
L-Lysine hydroxamate forward reaction, pH 8.0, 30°C Geobacillus stearothermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Geobacillus stearothermophilus

Cofactor

Cofactor Comment Organism Structure
ATP hyperbolic dependence of kapp on the initial ATP concentration, ATP binding to the enzyme-L-lysine complex follows a two-step mechanism Geobacillus stearothermophilus