BRENDA - Enzyme Database
show all sequences of 3.2.1.B41

Kinetic study of a thermostable beta-glycosidase of Thermus thermophilus. Effects of temperature and glucose on hydrolysis and transglycosylation reactions

Fourage, L.; Dion, M.; Colas, B.; Glycoconj. J. 17, 377-383 (2000)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
overexpressed in Escherichia coli
Thermus thermophilus
Inhibitors
Inhibitors
Commentary
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 [mM]
KM Value Maximum [mM]
Substrate
Commentary
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
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermus thermophilus
-
-
-
Purification (Commentary)
Commentary
Organism
-
Thermus thermophilus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4-nitrophenyl beta-D-cellobioside + H2O
-
747918
Thermus thermophilus
4-nitrophenyl beta-D-glucoside + D-glucose
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
-
747918
Thermus thermophilus
4-nitrophenol + beta-D-fucoside
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
-
747918
Thermus thermophilus
4-nitrophenol + D-galactose
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
-
747918
Thermus thermophilus
4-nitrophenol + D-glucose
-
-
-
?
cellotetraose + H2O
-
747918
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
747918
Thermus thermophilus
?
-
-
-
-
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
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
Cloned(Commentary) (protein specific)
Commentary
Organism
overexpressed in Escherichia coli
Thermus thermophilus
Inhibitors (protein specific)
Inhibitors
Commentary
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] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
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
Purification (Commentary) (protein specific)
Commentary
Organism
-
Thermus thermophilus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4-nitrophenyl beta-D-cellobioside + H2O
-
747918
Thermus thermophilus
4-nitrophenyl beta-D-glucoside + D-glucose
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
-
747918
Thermus thermophilus
4-nitrophenol + beta-D-fucoside
-
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
-
747918
Thermus thermophilus
4-nitrophenol + D-galactose
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
-
747918
Thermus thermophilus
4-nitrophenol + D-glucose
-
-
-
?
cellotetraose + H2O
-
747918
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
747918
Thermus thermophilus
?
-
-
-
-
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
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 [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
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
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
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
Other publictions for EC 3.2.1.B41
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
748250
Gu
Gene cloning and enzymatic pr ...
Thermus thermophilus, Thermus thermophilus HJ6
J. Biosci. Bioeng.
107
21-26
2009
-
-
1
-
-
-
-
8
1
-
3
-
-
5
-
-
1
-
-
-
-
-
8
1
1
1
1
8
1
1
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
8
1
-
3
-
-
-
-
1
-
-
-
-
8
1
1
1
1
8
1
1
-
1
-
-
-
-
8
8
747918
Fourage
Kinetic study of a thermostab ...
Thermus thermophilus
Glycoconj. J.
17
377-383
2000
-
-
1
-
-
-
1
4
-
-
-
-
-
3
-
-
1
-
-
-
-
-
6
-
-
-
-
3
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
4
-
-
-
-
-
-
-
1
-
-
-
-
6
-
-
-
-
3
-
-
-
-
-
-
-
-
3
3