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Literature summary extracted from

  • Hong, J.; Tamaki, H.; Kumagai, H.
    Unusual hydrophobic linker region of beta-glucosidase (BGLII) from Thermoascus aurantiacus is required for hyper-activation by organic solvents (2006), Appl. Microbiol. Biotechnol., 73, 80-88.
    View publication on PubMed

Activating Compound

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

Cloned(Commentary)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.21 D-glucose 50% inhibition at 1.39 M Thermoascus aurantiacus

KM Value [mM]

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.21 120000
-
His-tagged recombinant enzyme, native PAGE Thermoascus aurantiacus

Organism

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
-

Posttranslational Modification

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

Purification (Commentary)

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

Reaction

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.21 additional information
-
-
Thermoascus aurantiacus

Substrates and Products (Substrate)

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 ?
-
?

Subunits

EC Number Subunits Comment Organism
3.2.1.21 monomer 1 * 120000, His-tagged recombinant enzyme, SDS-PAGE Thermoascus aurantiacus

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.21 50
-
-
Thermoascus aurantiacus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.21 30 55
-
Thermoascus aurantiacus

Temperature Stability [°C]

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.21 5
-
-
Thermoascus aurantiacus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.21 3 9
-
Thermoascus aurantiacus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.21 3 8 purified His-tagged recombinant enzyme, quite stable Thermoascus aurantiacus

Ki Value [mM]

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