Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Geobacillus stearothermophilus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Geobacillus stearothermophilus | - |
- |
- |
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 | Comment | Organism |
---|---|---|
TrpRS | - |
Geobacillus stearothermophilus |
trytophanyl-tRNA synthetase | - |
Geobacillus stearothermophilus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Geobacillus stearothermophilus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Geobacillus stearothermophilus |