EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.21 | 2-butanol | 3fold activation | Thermoascus aurantiacus | |
3.2.1.21 | 2-Methyl-1-pentanol | addition of 20% v/v n-octanol results in a higher activity of 4-nitrophenyl-beta-D-glucopyranoside hydrolysis, and activation of transglycosylation activity, overview | Thermoascus aurantiacus | |
3.2.1.21 | 2-methyl-2-pentanol | addition of 20% v/v n-octanol results in a higher activity of 4-nitrophenyl-beta-D-glucopyranoside hydrolysis, and activation of transglycosylation activity, overview | Thermoascus aurantiacus | |
3.2.1.21 | 2-propanol | 9fold activation | Thermoascus aurantiacus | |
3.2.1.21 | 3-methyl-1-pentanol | addition of 20% v/v n-octanol results in an over 40fold higher activity of 4-nitrophenyl-beta-D-glucopyranoside hydrolysis, and activation of transglycosylation activity, overview | Thermoascus aurantiacus | |
3.2.1.21 | 4-Methyl-1-pentanol | addition of 20% v/v n-octanol results in a higher activity of 4-nitrophenyl-beta-D-glucopyranoside hydrolysis, and activation of transglycosylation activity, overview | Thermoascus aurantiacus | |
3.2.1.21 | acetone | hydrolysis activity is enhanced in the presence of non-acceptor type organic solvents such as hexane, cyclohexane, diethylether, and acetone | Thermoascus aurantiacus | |
3.2.1.21 | allyl alcohol | 6.7fold activation | Thermoascus aurantiacus | |
3.2.1.21 | Cyclohexane | hydrolysis activity is enhanced in the presence of non-acceptor type organic solvents such as hexane, cyclohexane, diethyl ether, and acetone | Thermoascus aurantiacus | |
3.2.1.21 | diethylether | hydrolysis activity is enhanced in the presence of non-acceptor type organic solvents such as hexane, cyclohexane, diethylether, and acetone | Thermoascus aurantiacus | |
3.2.1.21 | DMSO | 1.6fold activation | Thermoascus aurantiacus | |
3.2.1.21 | ethanol | high enzyme activation at 20-30% | Thermoascus aurantiacus | |
3.2.1.21 | hexane | hydrolysis activity is enhanced in the presence of non-acceptor type organic solvents such as hexane, cyclohexane, diethyl ether, and acetone | Thermoascus aurantiacus | |
3.2.1.21 | methanol | high enzyme activation at 20-30% | Thermoascus aurantiacus | |
3.2.1.21 | additional information | the hydrophobic linker region in BGLII is required for activation by organic solvents | Thermoascus aurantiacus | |
3.2.1.21 | n-butanol | 14fold activation | Thermoascus aurantiacus | |
3.2.1.21 | n-Heptanol | addition of 20% v/v n-octanol results in an over 40fold higher activity of 4-nitrophenyl-beta-D-glucopyranoside hydrolysis, and activation of transglycosylation activity, overview | Thermoascus aurantiacus | |
3.2.1.21 | n-Hexanol | addition of 20% v/v n-octanol results in an over 40fold higher activity of 4-nitrophenyl-beta-D-glucopyranoside hydrolysis, and activation of transglycosylation activity, overview | Thermoascus aurantiacus | |
3.2.1.21 | n-Octanol | addition of 20% v/v n-octanol results in a 54fold higher activity of 4-nitrophenyl-beta-D-glucopyranoside hydrolysis, and activation of transglycosylation activity, overview | Thermoascus aurantiacus | |
3.2.1.21 | n-Pentanol | 23fold activation | Thermoascus aurantiacus | |
3.2.1.21 | n-Propanol | 9.3fold activation | Thermoascus aurantiacus | |
3.2.1.21 | Triton X-100 | 4.5fold activation | Thermoascus aurantiacus | |
3.2.1.21 | Tween 20 | 5.5fold activation | Thermoascus aurantiacus | |
3.2.1.21 | Tween 80 | 3.6fold activation | Thermoascus aurantiacus |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.21 | gene bgl2, DNA and amino acid sequence determination and anaylsis, expression of a His-tagged cDNA fragment excluding the potential signal sequence in Pichia pastoris strain KM71H | Thermoascus aurantiacus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.21 | D-glucose | 50% inhibition at 1.39 M | Thermoascus aurantiacus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.21 | 0.02 | - |
4-nitrophenyl-beta-D-glucopyranoside | pH 5.0, 50°C, recombinant enzyme | Thermoascus aurantiacus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.2.1.21 | 120000 | - |
His-tagged recombinant enzyme, native PAGE | Thermoascus aurantiacus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.21 | Thermoascus aurantiacus | Q4U4W7 | gene bgl2 | - |
3.2.1.21 | Thermoascus aurantiacus IFO 9748 | Q4U4W7 | gene bgl2 | - |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.2.1.21 | glycoprotein | the enzyme contains nine potential N-glycosylation sites at Asn67, Asn75, Asn259, Asn330, Asn362, Asn423, Asn476, Asn644, and Asn661, removing the sugar chains of recombinant BGLII with Endo-H does not affect its properties including thermo-stability, optimal temperature, optimal pH, pH stability, and activation by organic solvents | Thermoascus aurantiacus |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.21 | recombinant His-tagged enzyme lacking the potential signal sequence from Pichia pastoris strain KM71H by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography | Thermoascus aurantiacus |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.2.1.21 | celloheptaose + 6 H2O = 7 beta-D-glucose | the conserved Asp287 is the potential nucleophile in the catalytic center | Thermoascus aurantiacus |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.2.1.21 | additional information | - |
- |
Thermoascus aurantiacus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.21 | 2-nitrophenyl beta-D-glucopyranoside + H2O | - |
Thermoascus aurantiacus | 2-nitrophenol + beta-D-glucose | - |
? | |
3.2.1.21 | 2-nitrophenyl beta-D-glucopyranoside + H2O | - |
Thermoascus aurantiacus IFO 9748 | 2-nitrophenol + beta-D-glucose | - |
? | |
3.2.1.21 | 4-nitrophenyl beta-D-cellobioside + 2 H2O | - |
Thermoascus aurantiacus | 4-nitrophenol + 2 beta-D-glucose | - |
? | |
3.2.1.21 | 4-nitrophenyl beta-D-glucopyranoside + H2O | - |
Thermoascus aurantiacus | 4-nitrophenol + beta-D-glucose | - |
? | |
3.2.1.21 | 4-nitrophenyl beta-D-glucopyranoside + H2O | - |
Thermoascus aurantiacus IFO 9748 | 4-nitrophenol + beta-D-glucose | - |
? | |
3.2.1.21 | 4-nitrophenyl beta-D-xylopyranoside + H2O | - |
Thermoascus aurantiacus | 4-nitrophenol + beta-D-xylose | - |
? | |
3.2.1.21 | 4-nitrophenyl beta-D-xylopyranoside + H2O | - |
Thermoascus aurantiacus IFO 9748 | 4-nitrophenol + beta-D-xylose | - |
? | |
3.2.1.21 | cellobiose + H2O | - |
Thermoascus aurantiacus | 2 beta-D-glucose | - |
? | |
3.2.1.21 | cellobiose + H2O | - |
Thermoascus aurantiacus IFO 9748 | 2 beta-D-glucose | - |
? | |
3.2.1.21 | cellooligosaccharides + H2O | - |
Thermoascus aurantiacus | beta-D-glucose | - |
? | |
3.2.1.21 | additional information | the recombinant enzyme BGLII has both beta-glucosidase and beta-xylosidase activity and shows transglycosylation activity with 4-nitrophenyl-beta-D-glucopyranoside as a donor and with various alcohols as acceptors, overview, no activity with carboxymethylcellulose | Thermoascus aurantiacus | ? | - |
? | |
3.2.1.21 | additional information | the recombinant enzyme BGLII has both beta-glucosidase and beta-xylosidase activity and shows transglycosylation activity with 4-nitrophenyl-beta-D-glucopyranoside as a donor and with various alcohols as acceptors, overview, no activity with carboxymethylcellulose | Thermoascus aurantiacus IFO 9748 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.2.1.21 | monomer | 1 * 120000, His-tagged recombinant enzyme, SDS-PAGE | Thermoascus aurantiacus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.21 | BglII | - |
Thermoascus aurantiacus |
3.2.1.21 | More | the enzyme belongs to the glycosyl hydrolase family 1 | Thermoascus aurantiacus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.21 | 50 | - |
- |
Thermoascus aurantiacus |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.21 | 30 | 55 | - |
Thermoascus aurantiacus |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.21 | 50 | - |
purified His-tagged recombinant enzyme, stable up to | Thermoascus aurantiacus |
3.2.1.21 | 60 | - |
purified His-tagged recombinant enzyme, rapid loss of activity | Thermoascus aurantiacus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.21 | 5 | - |
- |
Thermoascus aurantiacus |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.21 | 3 | 9 | - |
Thermoascus aurantiacus |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.21 | 3 | 8 | purified His-tagged recombinant enzyme, quite stable | Thermoascus aurantiacus |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.21 | 300 | - |
D-glucose | pH 5.0, 50°C, recombinant enzyme | Thermoascus aurantiacus |