Cloned (Comment) | Organism |
---|---|
overexpressed in Escherichia coli | Thermus thermophilus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | the substrate can act not only as a glycosyl donor but also as a glycosyl acceptor. In addition, when the glucose is added to reaction mixtures, inhibition or activation is observed depending on both substrate concentration and temperature. A reaction model is proposed to explain the kinetic behavior of the enzyme. The scheme integrates the inhibition observed at high concentrations of substrate and the activation due to transglycosylation reactions implicating the existence of a transfer subsite | Thermus thermophilus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | when the kinetics are performed below 60°C, the enzyme is inhibited by high substrate concentrations. At temperatures higher than 60°C, the inhibition phenomenon is no longer observed but, on the contrary, an activation is obtained at high substrate concentrations. Around 60°C, the enzyme displays Michaelian behavior | Thermus thermophilus | |
0.1 | - |
4-nitrophenyl beta-D-glucoside | 60°C, pH 7.0 | Thermus thermophilus | |
0.12 | - |
4-nitrophenyl beta-D-fucoside | 60°C, pH 7.0 | Thermus thermophilus | |
5.6 | - |
4-nitrophenyl beta-D-galactoside | 60°C, pH 7.0 | Thermus thermophilus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermus thermophilus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Thermus thermophilus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-nitrophenyl beta-D-cellobioside + H2O | - |
Thermus thermophilus | 4-nitrophenyl beta-D-glucoside + D-glucose | - |
? | |
4-nitrophenyl beta-D-fucoside + H2O | - |
Thermus thermophilus | 4-nitrophenol + beta-D-fucose | - |
? | |
4-nitrophenyl beta-D-galactoside + H2O | - |
Thermus thermophilus | 4-nitrophenol + D-galactose | - |
? | |
4-nitrophenyl beta-D-glucoside + H2O | - |
Thermus thermophilus | 4-nitrophenol + D-glucose | - |
? | |
cellotetraose + H2O | - |
Thermus thermophilus | cellotriose + D-glucose | - |
? | |
additional information | the enzyme is highly specific for beta-linked sugars. The substrate can act not only as a glycosyl donor but also as a glycosyl acceptor. In addition, when the glucose is added to reaction mixtures, inhibition or activation is observed depending on both substrate concentration and temperature. A reaction model is proposed to explain the kinetic behavior of the enzyme. The scheme integrates the inhibition observed at high concentrations of substrate and the activation due to transglycosylation reactions implicating the existence of a transfer subsite | Thermus thermophilus | ? | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
23.4 | - |
4-nitrophenyl beta-D-glucoside | 60°C, pH 7.0 | Thermus thermophilus | |
29.7 | - |
4-nitrophenyl beta-D-fucoside | 60°C, pH 7.0 | Thermus thermophilus | |
82.9 | - |
4-nitrophenyl beta-D-galactoside | 60°C, pH 7.0 | Thermus thermophilus |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
14.8 | - |
4-nitrophenyl beta-D-galactoside | 60°C, pH 7.0 | Thermus thermophilus | |
227 | - |
4-nitrophenyl beta-D-glucoside | 60°C, pH 7.0 | Thermus thermophilus | |
247 | - |
4-nitrophenyl beta-D-fucoside | 60°C, pH 7.0 | Thermus thermophilus |