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Literature summary extracted from

  • Fourage, L.; Dion, M.; Colas, B.
    Kinetic study of a thermostable beta-glycosidase of Thermus thermophilus. Effects of temperature and glucose on hydrolysis and transglycosylation reactions (2000), Glycoconj. J., 17, 377-383 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.B41 overexpressed in Escherichia coli Thermus thermophilus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.B41 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.B41 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
3.2.1.B41 0.1
-
 4-nitrophenyl beta-D-glucoside 60°C, pH 7.0 Thermus thermophilus
3.2.1.B41 0.12
-
 4-nitrophenyl beta-D-fucoside 60°C, pH 7.0 Thermus thermophilus
3.2.1.B41 5.6
-
 4-nitrophenyl beta-D-galactoside 60°C, pH 7.0 Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.B41 Thermus thermophilus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.B41
-
 Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.B41 4-nitrophenyl beta-D-cellobioside + H2O
-
 Thermus thermophilus 4-nitrophenyl beta-D-glucoside + D-glucose
-
 ?
3.2.1.B41 4-nitrophenyl beta-D-fucoside + H2O
-
 Thermus thermophilus 4-nitrophenol + beta-D-fucose
-
 ?
3.2.1.B41 4-nitrophenyl beta-D-galactoside + H2O
-
 Thermus thermophilus 4-nitrophenol + D-galactose
-
 ?
3.2.1.B41 4-nitrophenyl beta-D-glucoside + H2O
-
 Thermus thermophilus 4-nitrophenol + D-glucose
-
 ?
3.2.1.B41 cellotetraose + H2O
-
 Thermus thermophilus cellotriose + D-glucose
-
 ?
3.2.1.B41 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 [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.B41 23.4
-
 4-nitrophenyl beta-D-glucoside 60°C, pH 7.0 Thermus thermophilus
3.2.1.B41 29.7
-
 4-nitrophenyl beta-D-fucoside 60°C, pH 7.0 Thermus thermophilus
3.2.1.B41 82.9
-
 4-nitrophenyl beta-D-galactoside 60°C, pH 7.0 Thermus thermophilus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.2.1.B41 14.8
-
 4-nitrophenyl beta-D-galactoside 60°C, pH 7.0 Thermus thermophilus
3.2.1.B41 227
-
 4-nitrophenyl beta-D-glucoside 60°C, pH 7.0 Thermus thermophilus
3.2.1.B41 247
-
 4-nitrophenyl beta-D-fucoside 60°C, pH 7.0 Thermus thermophilus