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Literature summary for 6.1.1.11 extracted from

  • Samuelsson, T.; Lundvik, L.
    Purification and some properties of asparagine, lysine, serine, and valine:tRNA ligases from Bacillus stearothermophilus (1978), J. Biol. Chem., 253, 7033-7039.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information a temperature-dependent inhibition by conformational change of the enzyme (50°C-70°C) lowers both the catalytic activity and the substrate affinity of the ATP and amino acid sites as indicated by a sharp rise in Km with temperature Geobacillus stearothermophilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
49000
-
2 * 49000, SDS-PAGE Geobacillus stearothermophilus
81000
-
gel filtration, sedimentation velocity Geobacillus stearothermophilus
88000
-
sedimentation equilibrium measurement Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Geobacillus stearothermophilus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.106
-
-
Geobacillus stearothermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-serine + tRNASer
-
Geobacillus stearothermophilus AMP + diphosphate + L-seryl-tRNASer
-
?

Subunits

Subunits Comment Organism
dimer 2 * 49000, SDS-PAGE Geobacillus stearothermophilus

pH Range

pH Minimum pH Maximum Comment Organism
6 8 25°C, acylation rate increases when pH is raised from 6.0 to 8.0 Geobacillus stearothermophilus