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Literature summary for 6.1.1.2 extracted from

  • Weinreb, V.; Carter, C.W.
    Mg2+-free Bacillus stearothermophilus tryptophanyl-tRNA synthetase retains a major fraction of the overall rate enhancement for tryptophan activation (2008), J. Am. Chem. Soc., 130, 1488-1494.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + L-tryptophan + tRNATrp = AMP + diphosphate + L-tryptophyl-tRNATrp a nested, nonlinear model for the sum of metal-free and metal-catalyzed activities and its use in determining metal-free enzyme activity jointly with transition-state metal binding affinity is described, by fitting observed values obtained from Mg2+-depleted assays with increasing EDTA concentrations at known Mg2+ concentrations. Trp activation by TrpRS falls asymptotically to a plateau value 5 orders of magnitude below that observed for the Mg2+-supplemented enzyme at EDTA concentrations that reduce the free metal concentration to below 1 pmolar. The fitted regression model parameters yield a relative rate acceleration of 93000 attributable to the catalytic effect of Mg2+ and an enhanced transition state binding of Mg2+. Factorial analysis indicates that 80% of the reduction in free energy of activation effected by TrpRS arises from protein-ligand interactions Geobacillus stearothermophilus

Synonyms

Synonyms Comment Organism
TrpRS
-
Geobacillus stearothermophilus
trytophanyl-tRNA synthetase
-
Geobacillus stearothermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Geobacillus stearothermophilus

pH Optimum

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