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Literature summary 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]

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.1.1.6 57700
-
 2 * 57700, SDS-PAGE Geobacillus stearothermophilus
6.1.1.6 115400
-
 about Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.6 Geobacillus stearothermophilus
-
 NCA1503, purified enzyme
-

Reaction

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.6 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
6.1.1.6 ATP + L-lysine amide + tRNALys
-
 Geobacillus stearothermophilus AMP + L-amino-lysyl-tRNALys + diphosphate
-
 r
6.1.1.6 ATP + L-lysine hydroxamate + tRNALys
-
 Geobacillus stearothermophilus AMP + L-lysine hydroxamoyl-tRNALys + diphosphate
-
 r
6.1.1.6 ATP + lysine + tRNALys
-
 Geobacillus stearothermophilus AMP + L-lysyl-tRNALys + diphosphate
-
 r

Subunits

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.6 30
-
 assay at Geobacillus stearothermophilus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.6 additional information
-
 additional information hyperbolic dependence of kapp on the initial ATP concentration Geobacillus stearothermophilus
6.1.1.6 14.5
-
 L-Lysine amide forward reaction, pH 8.0, 30°C Geobacillus stearothermophilus
6.1.1.6 45.7
-
 L-lysine forward reaction, pH 8.0, 30°C Geobacillus stearothermophilus
6.1.1.6 221
-
 L-Lysine hydroxamate forward reaction, pH 8.0, 30°C Geobacillus stearothermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.6 8
-
 assay at Geobacillus stearothermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.6 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