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Information on EC 3.2.1.B28 - Pyrococcus furiosus beta-glycosidase
for references in articles please use BRENDA:EC3.2.1.B28preliminary BRENDA-supplied EC number
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EC Tree
3.2.1.B28 Pyrococcus furiosus beta-glycosidaseSpecify your search results
The expected taxonomic range for this enzyme is: Pyrococcus furiosus
Reaction Schemes
The enzyme produces mannose and glucose mainly from mannooligosaccharides and cellobiose by hydrolyzing them from the reducing end. It can not hydrolyze alpha-form substrates and bulk polymers like mannan and starch
Synonyms
pyrococcus furiosus beta-glycosidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CelB
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
The enzyme produces mannose and glucose mainly from mannooligosaccharides and cellobiose by hydrolyzing them from the reducing end. It can not hydrolyze alpha-form substrates and bulk polymers like mannan and starch
-
-
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,4-dinitrophenyl beta-D-glucopyranoside + H2O
2,4-dinitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + D-galactopyranose
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + D-galactopyranoside
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + D-galactose
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside-6-phosphate + H2O
2-nitrophenol + D-galactopyranoside-6-phosphate
-
-
-
?
2-nitrophenyl beta-D-galactoside
2-nitrophenol + D-galactose
-
-
-
r
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranoside
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucose
-
-
-
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + D-xylopyranose
-
-
-
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + L-arabinose
-
-
-
?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + L-arabinose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
catalytic efficiency (kcat/Km) for 4-nitrophenyl beta-D-galactopyranoside is 7.6% compared to catalytic catalytic efficiency (kcat/Km) for 4-nitrophenyl beta-D-glucopyranoside
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactopyranose
-
-
-
?
4-nitrophenyl beta-D-galactoside
4-nitrophenol + beta-D-galactose
CelB has a beta-galactosidase activity of 61% of the beta-glucosidase activity
-
-
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + D-galactose
at 80°C 61% of the activity with 4-nitrophenyl beta-D-glucoside
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucoside
4-nitrophenol + beta-D-glucose
CelB has a beta-galactosidase activity of 61% of the beta-glucosidase activity
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannopyranose
-
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannose
catalytic efficiency (kcat/Km) for 4-nitrophenyl beta-D-mannopyranoside is 0.7% compared to catalytic catalytic efficiency (kcat/Km) for 4-nitrophenyl beta-D-glucopyranoside
-
-
?
cellobiose + H2O
?
-
as active as 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
cellobiose + H2O
D-glucose + D-glucose
CelB is a little more active on the galactosides lactose and 4-nitrophenyl beta-D-galactopyranoside than on 4-nitrophenyl beta-D-glucopyranoside, whereas the efficiency of cellobiose hydrolysis is relatively low
-
-
?
D-glucose
gluco-oligosaccharides + H2O
-
study on the effect of pressure on the reaction equilibrium. Oligosaccharides are synthesized from glucose in an equilibrium reaction at pressures from 0.1 to 500 MPa. The enzyme remains active at 500 MPa. The equilibrium of the reaction is influenced by pressure and shifts towards the hydrolysis side, decreasing final oligosaccharide concentrations with increasing pressure. This pressure dependence of the final product concentration and the equilibrium constant can be described with a positive reaction volume of 2.4 mol/cm3
-
?
ginsenoside Rb1 + 4 H2O
protopanaxadiol aglycone + 4 D-glucopyranose
-
-
-
?
ginsenoside Rb2 + 4 H2O
protopanaxadiol aglycone + 3 D-glucopyranose + L-arabinopyranose
-
-
-
?
ginsenoside Rc + 4 H2O
protopanaxadiol aglycone + 3 D-glucopyranose + L-arabinopyranose
-
-
-
?
ginsenoside Rc + H2O
(3beta,12beta)-dammar-24-ene-3,12,20-triol + D-glucose + L-arabinofuranose
-
-
-
-
?
ginsenoside Rd + 3 H2O
protopanaxadiol aglycone + 3 D-glucopyranose
-
-
-
?
glycitin + H2O
beta-D-glucose + glycitein
i.e. glycitein 7-O-beta-glucoside
-
-
?
isoquercitrin + H2O
quercetin + beta-D-glucose
i.e. quercetin 3-O-beta-D-glucoside
-
-
?
lactose + N,N'-diacetylchitobiose
Gal-beta(1,4)-GlcNAc-beta(1,3)-Gal-beta(1,4)-Glc + H2O
-
-
-
?
mannooligosaccharide + H2O
?
hydrolysis of mannose from the reducing end
-
-
?
N-acetyl-D-glucosamine + lactose
4-O-beta-D-galactopyranosyl-N-acetyl-D-glucosamine + D-glucose
-
transgalactosylation reaction
-
?
pentyl beta-D-glucopyranoside + H2O
pentanol + beta-D-glucopyranose
-
-
-
?
quercitrin + H2O
quercetin + alpha-L-rhamnose
i.e. quercetin 3-O-alpha-L-rhamnoside
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
-
-
?
2-nitrophenyl beta-D-galactopyranoside + H2O
2-nitrophenol + beta-D-galactopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
37% of the activity compared to 4-nitrophenyl-beta-D-mannopyranoside
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
-
hydrolysed at 34% compared to activity with 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactose
CelB is a little more active on the galactosides lactose and 4-nitrophenyl beta-D-galactopyranoside than on 4-nitrophenyl beta-D-glucopyranoside, whereas the efficiency of cellobiose hydrolysis is relatively low
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
114% of the activity compared to 4-nitrophenyl-beta-D-mannopyranoside
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
CelB is a little more active on the galactosides lactose and 4-nitrophenyl beta-D-galactopyranoside than on 4-nitrophenyl beta-D-glucopyranoside, whereas the efficiency of cellobiose hydrolysis is relatively low
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
37% of the activity compared to 4-nitrophenyl-beta-D-mannopyranoside
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
hydrolysed at 9.2% compared to activity with 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
lactose + H2O
D-glucose + D-galactose
-
-
-
?
lactose + H2O
D-glucose + D-galactose
-
lactose is hydrolyzed into glucose and galactose, and then tri-, tetra-, and pentasaccharides are synthesized. The conversion rate for lactose increases with temperature, directly resulting in an increase in both the rate of hydrolysis and the rate of oligosaccharide synthesis. Because the increase in production rate is faster for oligosaccharide synthesis than for hydrolysis, relatively more oligosaccharides are produced at higher temperatures. At 50°C the optimum in oligosaccharide concentration, of which the occurrence is typical for a kinetically controlled reaction, is not yet reached after 250 h. At 95°C this optimum is reached within 4 h
-
r
lactose + H2O
D-glucose + D-galactose
CelB is a little more active on the galactosides lactose and 4-nitrophenyl beta-D-galactopyranoside than on 4-nitrophenyl beta-D-glucopyranoside, whereas the efficiency of cellobiose hydrolysis is relatively low
-
-
?
additional information
?
-
the enzyme also shows transglucosylation activity
-
-
?
additional information
?
-
the enzyme shows also beta-rutinosidase activity with rutin (hydrolysis of rutin to quercetin and rutinose)
-
-
?
additional information
?
-
the enzyme shows transglycosylation and transgalactosylation activities toward cellobiose, lactose and mannooligosaccharides that could produce galactooligosaccharides and maltooligosaccharides. It can not hydrolyze alpha-form substrates and bulk polymers like mannan and starch
-
-
?
additional information
?
-
the transferase activity of the enzyme can be improved significantly by addition of the ionic liquid 1,3-dimethylimidazoliummethylsulfate. The relative enhancement of the selectivity of the enzyme for glycosyl transfer to the acceptor nucleophile compared with water by the cosolvent is strongly dependent on the structure of the acceptor, suggesting that interactions of the acceptor with solvent molecules, water or ionic liquid, make a major contribution to the observed transgalactosylation specificity of the enzyme
-
-
?
additional information
?
-
the enzyme catalyzes the conversion of lactose to hexyl-beta-galactoside in hexanol (transgalactosylation reaction)
-
-
?
additional information
?
-
the transfer of the galactosyl group from lactose to acceptors such as lactose or D-glucose rather than water is significant and depends on the initial lactose concentration as well as the time-dependent substrate/product ratio during batchwise lactose conversion
-
-
?
additional information
?
-
enzyme additionally catalyzes transglycosylation reactions, making new beta(1->3) and beta(1->6) glycosidic bonds by intermolecular as well as intramolecular transfer reactions. The intramolecular galactosyl transfer of CelB yields beta-D-Galp-(1->6)-D-glucose and beta-D-Galp-(1->3)-D-glucose in a molar ratio of about 1 : 2. Galactosyl transfer from CelB to D-glucose occurs with partitioning ratios, kNu /kwater, which are 170 times those for the reactions of the galactosylated enzyme with 2-propanol. Therefore, the binding interactions with nucleophiles contribute chiefly to formation of new beta-glycosides during lactose conversion. Likewise, noncovalent interactions with the glucose leaving group govern the catalytic efficiencies for the hydrolysis of lactose
-
-
?
additional information
?
-
enzyme catalyzes both hydrolysis and transglycosylation of glycosidc substrates. In hexanol/water two-phase systems, hydrolysis is by far the dominating reaction even though the total activity increases. In hexanol containing various amounts of water, the selectivity for the alcohol increases with increasing water activity. This counteracts the effect of higher water concentration and the transglycosylation/hydrolysis ratio increases with increasing water activity
-
-
?
additional information
?
-
enzyme converts ginsenosides Rb1, Rb2, Rc, and Rd to protopanaxadiol aglycone via compound K
-
-
?
additional information
?
-
enzyme is able to catalyze formation of lacto-N-neotetraose, i.e. Gal-beta(1,4)-GlcNAc-beta(1,3)-Gal-beta(1,4)-Glc, from lactose and N,N'-diacetylchitobiose and of N-acetyllactosamine, i.e Gal-beta(1,4)-GlcNAc from N-acetylglucosamine and lactose. When compared with beta-glycosidase BglT from Thermus thermophilus, and beta-galactosidase BgaD-D from Bacillus circulans, BgaD is the most potent transgalactosidase, but both BglT and CelB can catalyze formation of LNnT and LacNAc, with BglT giving higher yields than CelB
-
-
?
additional information
?
-
enzyme shows transglucosylation activity with glucosyl donors 2-nitrophenyl beta-D-glucoside and cellobiose. Transglucosylation products are 1-O-beta-D-glucopyranosyl-rac-glycerol (79%) and 2-O-beta-D-glucopyranosyl-sn-glycerol (21%)
-
-
?
additional information
?
-
-
the enzyme also contains alpha-L-arabinofuranosidase activity
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
1,3-dimethylimidazolium methylsulfate
the enzyme retains full catalytic efficiency for lactose hydrolysis at 80°C in a 50% (v/v) solution of the ionic liquid 1,3-dimethylimidazoliummethylsulfate in sodium citrate buffer, pH 5.5. It is inactive but not irreversibly denatured at 70% (v/v) ionic liquid
(5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
-
(5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
inhibits activity with 4-nitrophenyl beta-D-galactopyranoside
D-glucose
inhibits activity with 4-nitrophenyl beta-D-galactopyranoside
D-glucose
measured with 2-nitrophenyl beta-D-galactoside as the substrate
SDS
0.03%, 50% residual activity. 0.04% less than 10% residual activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
not activated by monovalent or divalent cations
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.3
2-nitrophenyl beta-D-galactoside
release of 2-nitrophenol, pH 7.5, 80°C
46
pentyl beta-D-glucopyranoside
pH 5.0, 80°C, 6% water, 94% hexanol
additional information
additional information
mutants enzymes R77Q and R77Q/N206D show a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
-
0.89
2-nitrophenyl beta-D-galactopyranoside
mutant F426Y, pH 5.0, 90°C
2.3
2-nitrophenyl beta-D-galactopyranoside
wild-type, pH 5.0, 90°C
4.8
2-nitrophenyl beta-D-galactopyranoside
mutant M424K, pH 5.0, 90°C
40
2-nitrophenyl beta-D-galactopyranoside
mutant E417S/M424K/F426Y, pH 5.0, 90°C
42
2-nitrophenyl beta-D-galactopyranoside
mutant E417S, pH 5.0, 90°C
16
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
mutant E417S/M424K/F426Y, pH 5.0, 90°C
22
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
mutant E417S, pH 5.0, 90°C
31
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
wild-type, pH 5.0, 90°C
38
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
mutant F426Y, pH 5.0, 90°C
0.1
2-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
0.22
2-nitrophenyl beta-D-glucopyranoside
wild-type, pH 6.5, 65°C, presence of 2 M formate
0.3
2-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q150W
0.51
2-nitrophenyl beta-D-glucopyranoside
mutant M424K, pH 5.0, 90°C
0.57
2-nitrophenyl beta-D-glucopyranoside
mutant F426Y, pH 5.0, 90°C
1.3
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 5.0, 65°C
1.49
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 6.5, 65°C, presence of 2 M formate
2.1
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 4.0, 65°C
4.3
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 3.0, 65°C
29
2-nitrophenyl beta-D-glucopyranoside
mutant E417S, pH 5.0, 90°C
59
2-nitrophenyl beta-D-glucopyranoside
mutant E417S/M424K/F426Y, pH 5.0, 90°C
0.7
4-nitrophenyl beta-D-galactopyranoside
wild-type, pH 4.8, 20°C
1.2
4-nitrophenyl beta-D-galactopyranoside
mutant N4515S, pH 4.8, 20°C
1.3
4-nitrophenyl beta-D-galactopyranoside
mutant T371A, pH 4.8, 20°C
3.4
4-nitrophenyl beta-D-galactopyranoside
mutant M424V, pH 4.8, 20°C
4.5
4-nitrophenyl beta-D-galactopyranoside
mutant A419T, pH 4.8, 20°C
5
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, wild-type enzyme
8.5
4-nitrophenyl beta-D-galactopyranoside
mutant N4515S, pH 4.8, 90°C
15.7
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, mutant enzyme N206D
21.7
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, mutant enzyme R77Q
22
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D
0.02
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
0.05
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q150W
0.19
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, wild-type enzyme
0.39
4-nitrophenyl beta-D-glucopyranoside
90°C, pH not specified in the publication, enzyme from Pyrococcus furiosus
0.39
4-nitrophenyl beta-D-glucopyranoside
pH 6.5, temperature not specified in the publication, recombinant enzyme
0.41
4-nitrophenyl beta-D-glucopyranoside
90°C, pH not specified in the publication, enzyme expressed in Escherichia coli
0.41
4-nitrophenyl beta-D-glucopyranoside
pH 6.5, temperature not specified in the publication, enzyme purified from Pyrococcus furiosus
0.57
4-nitrophenyl beta-D-glucopyranoside
mutant T371A, pH 4.8, 20°C
0.92
4-nitrophenyl beta-D-glucopyranoside
mutant M424V, pH 4.8, 20°C
1.1
4-nitrophenyl beta-D-glucopyranoside
mutant N4515S, pH 4.8, 20°C
1.3
4-nitrophenyl beta-D-glucopyranoside
mutant A419T, pH 4.8, 20°C
1.4
4-nitrophenyl beta-D-glucopyranoside
mutant N4515S, pH 4.8, 90°C
4.6
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, mutant enzyme N206D
13.8
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, mutant enzyme R77Q
13.9
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D
21
4-nitrophenyl beta-D-glucoside
pH 5.0, 95°C, mutant enzyme F426Y
27
4-nitrophenyl beta-D-glucoside
pH 5.0, 95°C, mutant enzyme M424K/F426Y
39
4-nitrophenyl beta-D-glucoside
pH 5.0, 95°C, mutant enzyme M424K
0.03
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
0.05
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 95°C, mutant enzyme Q150W
0.1
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D, below 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
0.15
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q, below 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
0.63
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme N206D
0.64
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q, above 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
1.3
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, wild-type enzyme
1.5
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D, above 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10000
2-nitrophenyl beta-D-galactoside
release of 2-nitrophenol, pH 7.5, 80°C
additional information
additional information
mutants enzymes R77Q and R77Q/N206D show a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
-
20 - 50
2-nitrophenyl beta-D-galactopyranoside
wild-type, pH 5.0, 90°C
175
2-nitrophenyl beta-D-galactopyranoside
mutant E417S/M424K/F426Y, pH 5.0, 90°C
892
2-nitrophenyl beta-D-galactopyranoside
mutant F426Y, pH 5.0, 90°C
1060
2-nitrophenyl beta-D-galactopyranoside
mutant E417S, pH 5.0, 90°C
1880
2-nitrophenyl beta-D-galactopyranoside
mutant M424K, pH 5.0, 90°C
26
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
mutant F426Y, pH 5.0, 90°C
49
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
wild-type, pH 5.0, 90°C
69
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
mutant E417S/M424K/F426Y, pH 5.0, 90°C
171
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
mutant E417S, pH 5.0, 90°C
0.22
2-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
0.45
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 5.0, 65°C
0.67
2-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q150W
3.9
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 6.5, 65°C, presence of 2 M formate
6.7
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 4.0, 65°C
47.6
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 3.0, 65°C
772
2-nitrophenyl beta-D-glucopyranoside
mutant M424K, pH 5.0, 90°C
777
2-nitrophenyl beta-D-glucopyranoside
mutant E417S/M424K/F426Y, pH 5.0, 90°C
840
2-nitrophenyl beta-D-glucopyranoside
mutant F426Y, pH 5.0, 90°C
1189
2-nitrophenyl beta-D-glucopyranoside
wild-type, pH 6.5, 65°C, presence of 2 M formate
3300
2-nitrophenyl beta-D-glucopyranoside
mutant E417S, pH 5.0, 90°C
4.2
4-nitrophenyl beta-D-galactopyranoside
mutant N4515S, pH 4.8, 20°C
9.1
4-nitrophenyl beta-D-galactopyranoside
wild-type, pH 4.8, 20°C
11
4-nitrophenyl beta-D-galactopyranoside
mutant T371A, pH 4.8, 20°C
12
4-nitrophenyl beta-D-galactopyranoside
mutant M424V, pH 4.8, 20°C
14
4-nitrophenyl beta-D-galactopyranoside
mutant A419T, pH 4.8, 20°C
29.2
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D
69.2
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, mutant enzyme R77Q
180
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, mutant enzyme N206D
1000
4-nitrophenyl beta-D-galactopyranoside
mutant N4515S, pH 4.8, 90°C
2400
4-nitrophenyl beta-D-galactopyranoside
wild-type, pH 4.8, 90°C
2827
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, wild-type enzyme
0.05
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
0.13
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q150W
26
4-nitrophenyl beta-D-glucopyranoside
mutant T371A, pH 4.8, 20°C
40
4-nitrophenyl beta-D-glucopyranoside
mutant A419T, pH 4.8, 20°C
40
4-nitrophenyl beta-D-glucopyranoside
mutant M424V, pH 4.8, 20°C
47
4-nitrophenyl beta-D-glucopyranoside
mutant N4515S, pH 4.8, 20°C
116
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, mutant enzyme N206D
172
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D
207
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, mutant enzyme R77Q
1140
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, wild-type enzyme
1400
4-nitrophenyl beta-D-glucopyranoside
mutant N4515S, pH 4.8, 90°C
0.8
4-nitrophenyl beta-D-glucoside
pH 5.0, 95°C, mutant enzyme M424K/F426Y
0.9
4-nitrophenyl beta-D-glucoside
pH 5.0, 95°C, mutant enzyme F426Y
5
4-nitrophenyl beta-D-glucoside
pH 5.0, 95°C, mutant enzyme M424K
0.11
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
0.13
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 95°C, mutant enzyme Q150W
0.85
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q, below 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
1.02
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D, below 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
1.22
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q, above 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
1.9
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D, above 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
1.97
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme N206D
65.9
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1900
2-nitrophenyl beta-D-galactoside
release of 2-nitrophenol, pH 7.5, 80°C
additional information
additional information
mutants enzymes R77Q and R77Q/N206D show a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
-
4.4
2-nitrophenyl beta-D-galactopyranoside
mutant E417S/M424K/F426Y, pH 5.0, 90°C
25.3
2-nitrophenyl beta-D-galactopyranoside
mutant E417S, pH 5.0, 90°C
396
2-nitrophenyl beta-D-galactopyranoside
mutant M424K, pH 5.0, 90°C
899
2-nitrophenyl beta-D-galactopyranoside
wild-type, pH 5.0, 90°C
1000
2-nitrophenyl beta-D-galactopyranoside
mutant F426Y, pH 5.0, 90°C
0.7
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
mutant F426Y, pH 5.0, 90°C
1.6
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
wild-type, pH 5.0, 90°C
4.2
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
mutant E417S/M424K/F426Y, pH 5.0, 90°C
7.7
2-nitrophenyl beta-D-galactopyranoside-6-phosphate
mutant E417S, pH 5.0, 90°C
0.3
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 5.0, 65°C
2.17
2-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
2.26
2-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q150W
2.6
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 6.5, 65°C, presence of 2 M formate
3.1
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 4.0, 65°C
10.9
2-nitrophenyl beta-D-glucopyranoside
mutant E372A, pH 3.0, 65°C
13
2-nitrophenyl beta-D-glucopyranoside
mutant E417S/M424K/F426Y, pH 5.0, 90°C
113
2-nitrophenyl beta-D-glucopyranoside
mutant E417S, pH 5.0, 90°C
1484
2-nitrophenyl beta-D-glucopyranoside
mutant F426Y, pH 5.0, 90°C
1510
2-nitrophenyl beta-D-glucopyranoside
mutant M424K, pH 5.0, 90°C
5350
2-nitrophenyl beta-D-glucopyranoside
wild-type, pH 6.5, 65°C, presence of 2 M formate
1.3
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D
3.1
4-nitrophenyl beta-D-galactopyranoside
mutant A419T, pH 4.8, 20°C
3.2
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, mutant enzyme R77Q
3.4
4-nitrophenyl beta-D-galactopyranoside
mutant M424V, pH 4.8, 20°C
3.5
4-nitrophenyl beta-D-galactopyranoside
mutant N4515S, pH 4.8, 20°C
8.2
4-nitrophenyl beta-D-galactopyranoside
mutant T371A, pH 4.8, 20°C
11.5
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, mutant enzyme N206D
120
4-nitrophenyl beta-D-galactopyranoside
mutant N4515S, pH 4.8, 90°C
480
4-nitrophenyl beta-D-galactopyranoside
wild-type, pH 4.8, 90°C
561
4-nitrophenyl beta-D-galactopyranoside
pH 5.0, 90°C, wild-type enzyme
2.44
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q150W
2.95
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
12.3
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D
14.9
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, mutant enzyme R77Q
24.9
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, mutant enzyme N206D
31
4-nitrophenyl beta-D-glucopyranoside
mutant A419T, pH 4.8, 20°C
43
4-nitrophenyl beta-D-glucopyranoside
mutant M424V, pH 4.8, 20°C
43
4-nitrophenyl beta-D-glucopyranoside
mutant N4515S, pH 4.8, 20°C
45
4-nitrophenyl beta-D-glucopyranoside
mutant T371A, pH 4.8, 20°C
1000
4-nitrophenyl beta-D-glucopyranoside
mutant N4515S, pH 4.8, 90°C
7337
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, wild-type enzyme
1.3
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D, above 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
1.9
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q, above 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
2.83
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 95°C, mutant enzyme Q150W
3.1
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme N206D
3.63
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 95°C, mutant enzyme Q77R/Q150W
5.7
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q, below 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
10.2
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, mutant enzyme R77Q/N206D, below 1 mM 4-nitrophenyl beta-D-mannopyranoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
49.8
4-nitrophenyl beta-D-mannopyranoside
pH 5.0, 90°C, wild-type enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000065 - 0.0098
(5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
0.0000065
(5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
pH 5.0, 90°C, wild-type enzyme
0.0000093
(5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
pH 5.0, 70°C, substrate: 4-nitrophenyl beta-D-galactopyranoside
0.000097
(5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
pH 5.0, 90°C, mutant enzyme R77Q
0.0027
(5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
pH 5.0, 90°C, mutant enzyme R77Q/N206D
0.0098
(5R,6R,7S,8S)-5-(hydroxymethyl)-2-phenyl-5,6,7,8-tetrahydroimidazol[1,2-a]pyridine-6,7,8-triol
pH 5.0, 90°C, mutant enzyme N206D
43
D-glucose
pH 5.0, 70°C, substrate: 4-nitrophenyl beta-D-galactopyranoside
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.08
0.28
mutant E372A, substrate 2-nitrophenyl beta-D-xylopyranoside, pH 3.0, 65°C
1049
wild-type, substrate 2-nitrophenyl beta-D-galactopyranoside, pH 3.0, 65°C
15
substrate 4-nitrophenyl alpha-L-arabinopyranoside, pH 5.5, 95°C
291
wild-type, substrate 4-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
320
wild-type, substrate 2,4-dinitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
4.5
4.7
mutant E372A, substrate 2-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
529
substrate 2-nitrophenyl beta-D-galactopyranoside, pH 5.5, 95°C
534
wild-type, substrate 2-nitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
561
substrate 4-nitrophenyl beta-D-galactopyranoside, pH 5.5, 95°C
75
8.3
mutant E372A, substrate 2,4-dinitrophenyl beta-D-glucopyranoside, pH 3.0, 65°C
912
0.08
mutant E372A, substrate 2-nitrophenyl beta-D-galactopyranoside, pH 3.0, 65°C
4.5
substrate 4-nitrophenyl alpha-L-arabinofuranoside, pH 5.5, 95°C
75
wild-type, substrate 2-nitrophenyl beta-D-xylopyranoside, pH 3.0, 65°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
wild-type, substrate 2-nitrophenyl beta-D-galactopyranoside-6-phosphate
5.5
5
mutant E417S/M424K/F426Y, substrates 2-nitrophenyl beta-D-glucopyranoside, 2-nitrophenyl beta-D-galactopyranoside
5
wild-type, substrates 2-nitrophenyl beta-D-glucopyranoside, 2-nitrophenyl beta-D-galactopyranoside
6
mutant E417S/M424K/F426Y, substrate 2-nitrophenyl beta-D-galactopyranoside-6-phosphate
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 6
pH 4.5: about 85% of maximal activity, pH 6.0: about 60% of maximal activity
4.5 - 6.5
pH 4.5: about 50% of maximal activity, pH 6.5: about 60% of maximal activity, substrate: hesperidin
5 - 7
pH 5.0: 80% of maximal activity, pH 8.0: about 80% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
95
additional information
CelB shows almost constant selcetivity for the glycon part of a donor substrate as the temperature increases. The specificity constant (Vmax/Km) ratio of phenyl-beta-glucoside and phenyl-beta-galactoside substrate decreases only slightly from 2.6 to 2.1 between 50 and 90°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70 - 110
70°C: about 50% of maximal activity, 110°C: about 45% of maximal activity
75 - 95
the activity increases from 75°C to 95°C, activity at 75°C is about 40% of the activity at 95°C, substrate: hesperidin
75 - 98
75°C: about 50% of maximal activity, 98°C: about 85% of maximal activity
80 - 110
-
80°C: about 45% of maximal activity, 110°C: about 65% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q8U3U9_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
483
0
56327
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
230000
55488
56000
57000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dodecamer
a monomeric form of the enzyme is constructed by removing the C-terminal region of the enzyme (the mutant lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449K). The mutant enzyme forms a unique dodecameric structure consisting of two hexameric rings in the asymmetric unit of the crystal
monomer
a monomeric form of the enzyme is constructed by removing the C-terminal region of the enzyme (the mutant lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449K). The mutant enzyme forms a unique dodecameric structure consisting of two hexameric rings in the asymmetric unit of the crystal
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3.3 A resolution structural model. CelB shows a homo-tetramer configuration, with subunits having a typical (betaalpha)8-barrel fold
hanging-drop vapour-diffusion method, a monomeric form of the enzyme is constructed by removing the C-terminal region (the mutant lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449K) of the enzyme and its crystal structure is solved at a resolution of 2.8 A in space group
to 2.35 A resolution. There is one tetramer in the asymmetric unit and the dimeric molecule exhibits a structure that is stable towards sodium dodecyl sulfate even after boiling at 368 K. The elongation at the C-terminal end forms a hydrophobic patch at the dimer interface that might contribute to hyperthermostability
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A419T
159% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 109% with 4-nitrophenyl beta-D-galactoside, 53% residual activity after 1 h at 106°C
E386G
mutation in nucleophile residue E387, mutation completely abolishes activity under statndard conditions. The addition of 2 M sodium formate as an external nucleophile leads to the recovery of 8.40% activity with accumulation of oligosaccharides. At pH 3.0 and low concentrations of sodium formate buffer, the hyperthermophilic glycosynthase shows kcat values similar to those of the wild-type and 17fold higher than those observed at the usual reactivation conditions in 2 M sodium formate at pH 6.5
E417S
mutation in phosphate binding site, 5fold increase of the efficiency of hydrolyzing o-nitrophenol-beta-D-galactopyranoside-6-phosphate. Activity on nonphosphorylated sugars is largely reduced
E417S/M424K/F426Y
mutations in phosphate binding site, 3fold increase of the efficiency of hydrolyzing 2-nitrophenyl beta-D-galactopyranoside-6-phosphate. Activity on nonphosphorylated sugars is largely reduced
F426Y
I161V
110% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 37% with 4-nitrophenyl beta-D-galactoside, 84% residual activity after 1 h at 106°C
I67T
110% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 97% with 4-nitrophenyl beta-D-galactoside, 100% residual activity after 1 h at 106°C
K285R
155% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 103% with 4-nitrophenyl beta-D-galactoside, 58% residual activity after 1 h at 106°C
K70R
175% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 147% with 4-nitrophenyl beta-D-galactoside, 1% residual activity after 1 h at 106°C
M424K
M424K/F426Y
mutant has lower activity than the wild-type enzyme, but provides a higher ratio of transglucosylation product to hydrolysis products compared to wild-type enzyme
M424V
199% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 140% with 4-nitrophenyl beta-D-galactoside, 24% residual activity after 1 h at 106°C
N206N
about 300fold decrease in catalytic efficiency for 4-nitrophenyl-beta-D-glucospyranoside, about 50fold decrease in catalytic efficiency for 4-nitrophenyl-beta-D-galactoside
N415S
259% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 64% with 4-nitrophenyl beta-D-galactoside. 7.5fold increase in the ratio of 4-nitrophenyl beta-D-glucopyranoside/p-nitrophenyl beta-D-galactopyranoside hydrolysis, no decrease in thermostability
Q150W
the mutant enzyme has more affinity (Km) towards each substrate but shows lower turnover number (kcat) compared to the wild-type enzyme
Q77R/Q150W
the mutant enzyme has more affinity (Km) towards each substrate but shows lower turnover number (kcat) compared to the wild-type enzyme
R77Q
2000fold decrease in catalytic efficiency for 4-nitrophenyl-beta-D-glucospyranoside, 175fold decrease in catalytic efficiency for 4-nitrophenyl-beta-D-galactoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
R77Q/N206D
about 600fold decrease in catalytic efficiency for 4-nitrophenyl-beta-D-glucospyranoside, about 430fold decrease in catalytic efficiency for 4-nitrophenyl-beta-D-galactoside. The mutant enzyme shows a biphasic behavior for the hydrolysis of 4-nitrophenyl beta-D-mannopyranoside with separate kinetic parameters above and below 1 mM 4-nitrophenyl beta-D-mannopyranoside
T371A
148% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 149% with 4-nitrophenyl beta-D-galactoside, 14% residual activity after 1 h at 106°C
V211A
260% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 151% with 4-nitrophenyl beta-D-galactoside, 1% residual activity after 1 h at 106°C
additional information
F426Y
mutant has lower activity than the wild-type enzyme, but provides a higher ratio of transglucosylation product to hydrolysis products compared to wild-type enzyme, 2.6fold increase. The mutant enzyme has higher selectivity over the wide range of temperatures tested
F426Y
mutation in phosphate binding site, results in an increased affinity for galactosides. Activity on nonphosphorylated sugars is largely reduced
M424K
mutant has lower activity than the wild-type enzyme, but provides a higher ratio of transglucosylation product to hydrolysis products compared to wild-type enzyme
M424K
mutation in phosphate binding site, shifting pH optimum from 5.0 to 6.0. Activity on nonphosphorylated sugars is largely reduced
additional information
generation of functional glycoside hydrolase hybrids by shuffling of the genes coding for Pyrococcus furiosus CelB and Sulfolobus solfataricus LacS. Generating of thermostable hybrid beta-glycosidases and isolating high-performance variants
additional information
a mutant lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449K forms a unique dodecameric structure consisting of two hexameric rings in the asymmetric unit of the crystal. The lack of the C-terminal region does not affect the activity of the enzyme, but disrupts its oligomeric state and hyperthermostability
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
106
110
70
75
75 - 80
the mutant enzyme that lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449K is immediately inactivated between 75 and 80°C
80
85
90
95
additional information
thermostability is not affected by the presence of Mg2+
100
30 h, enzyme produced by Escherichia coli retains 80% of its activity, enzyme from Pyrococcus furiosus retains 90% of its activity
100
30 h, enzyme purified from Pyrococcus furiosus and recombinant enzyme retains 80 to 90% of the initial activity
80
at reaction temperatures of 80°C and higher, the inactivation rate of the enzyme in the presence of sugars is increased by a factor of 2, caused by the occurrence of Maillard reactions between the sugar and the enzyme
90
protein unfolds at 90°C with an overall DELTAG° of about 20 kcal/mol. Unfolding proceeds via a three-state pathway that includes a stable intermediate species. Stability of the native and intermediate forms is concentration dependen. A model for the denaturation of beta-glucosidase predicts that the tetramer dissociates to partially folded dimers, followed by the coupled dissociation and denaturation of the dimers to unfolded monomers
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
chaotropes (I-, ClO4-, NO3- and Cs+) have a strong destabilising effect on the protein by perturbing hydrophobic interactions
half-life of free enzyme is 680 h in absence and 22 h in presence of 1 M glucose, half-life of cross-linked enzyme is 18 h in absence and 3 h in presence of 1 M glucose, half-life of cross-linked cells is 840 h in absence and 47 h in presnce of 1 M glucose, respectively
half-life times of the enzyme in hydrolysis of lactose is carried out at 70°C in a continuous stirred-tank reactor coupled to a 10000 Da cross-flow ultrafiltration module (to recycle the enzyme) is approximately 5 to 7 days
the enzyme can be immobilized with little loss of enzyme activity and catalytic efficiency by covalent coupling of the proteins via the surface amino groups to insoluble carriers
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexanol
enzyme catalyzes both hydrolysis and transglycosylation of glycosidc substrates. In hexanol/water two-phase systems, hydrolysis is by far the dominating reaction even though the total activity increases. In hexanol containing various amounts of water, the selectivity for the alcohol increases with increasing water activity. This counteracts the effect of higher water concentration and the transglycosylation/hydrolysis ratio increases with increasing water activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli, mutant enzymes Q150W and Q77R/Q150W
expression in in Lactobacillus plantarum NC8 and Lactobacillus casei as hosts. Both lactobacilli harboring the pSIP409-celB vector produce active CelB in batch bioreactor cultivations while the specific CelB activity of the cell free extract is about 44% higher with Lactobacillus plantarum than with Lactobacillus casei using 4-nitrophenyl beta-galactoside as the substrate. A fedbatch bioreactor cultivation of Lactobacillus plantarum NC8 pSIP409-celB results in a specific CelB activity of 2500 nkat 4-nitrophenyl beta-D-galactopyranoside/mg protein after 28 h. A repeated dosage of the inducer (sakacin P inducing peptide) does not increase the enzyme expression further
expression of wild-type enzyme and mutant enzymes in Escherichia coli
expression using a baculovirus expression vector system in silkworm, Bombyx mori
overexpressed in Escherichia coli, resulting in high-level (up to 20% of total protein) production of the enzyme
recombinant mutant that lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449Kis expressed in Escherichia coli BL21
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
during growth of Pyrococcus furiosus on either cellobiose or laminarin, the activities of both beta-glucosidase and endoglucanase are increased at least fivefold compared with levels during growth on maltose or pyruvate, due to an enhanced transcription of both the celB gene and the lamA operon in the presence of these glucose-containing substrates
gene locus includes the celB gene, and a divergently orientated gene cluster, adhA-adhB-lamA, which codes for two alcohol dehydrogenases and an extracellular beta-1,3-endoglucanase. The in vivo and in vitro transcription initiation sites of both the celB gene and the lamA operon lie 25 nucleotides downstream of conserved TATA box motifs
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
encapsulation of CelB into silica microcapsules for degradation of biomass. The encapsulated enzyme is active at 80-100°C, but diffusion of cellobiose into the silica microcapsules is a rate-limiting step
food industry
pharmacology
the hyperthermostable beta-glycosidase may be useful for food and pharmaceutical applications
synthesis
additional information
the enzyme converts flavanone glycoside to flavanone aglycone via a one-step reaction. It may be useful in the production of the flavanone aglycones naringenin and hesperetin from flavanone glycosides in citrus extracts
food industry
the hyperthermostable beta-glycosidase may be useful for food and pharmaceutical applications
food industry
the enzyme suitable for hydrolysis of lactose at temperatures at 70-80°C
food industry
-
the immobilized enzyme is useful for the hydrolysis of lactose in whey or milk by using a packed-bed enzyme reactor operated at 70°C
synthesis
a continuous stirred-tank reactor charged with the enzyme and operated at steady-state conditions could be a useful reaction system for the production of galacto-oligosaccharides in which composition is narrower and more easily programmable, in terms of the individual components contained, as compared to the batchwise reaction
synthesis
optimization of hexyl-beta-glycoside synthesis from lactose in hexanol at low water activity and high temperature. Compared to other beta-glycosidases in lactose conversion into alkyl glycoside, the enzyme shows high activity in a hexanol one-phase system and synthesized high yields of both hexyl-beta-galactoside and hexyl-beta-glucoside. The enzyme synthesizes yields of 63% galactoside (58.6mM) and 28% glucoside (26.1 mM)
synthesis
-
the immobilized enzyme is useful for the production of galactooligosaccharides by using a packed-bed enzyme reactor operated at 70°C
synthesis
beta-glycosidase converts ginsenosides Rb1, Rb2, Rc, and Rd to protopanaxadiol aglycone via compound K. With increases in the enzyme activity, the productivities increase. The substrate concentration is optimal at ginsenoside Rd or 10% (w/v) ginseng root extract. 4 mM of ginsenoside Rd is converted to 3.3 mM compound K with a yield of 82.5% (mol/mol) and a productivity of 2010 mg per l and h at 1 h and is hydrolyzed completely to the aglycone with 364 mg per l and h after 5 h
synthesis
continuous enzymatic process for the production of the prebiotic disaccharide lactulose through transgalactosylation by CelB. CelB is immobilized onto anion-exchange resin Amberlite IRA-93 or onto Eupergit C with immobilization yields of 72% and 83%, respectively, giving specific activities of 920 nkat/g dry carrier and 1500 nkat/g dry carrier at 75°C with 4-nitrophenyl-beta-D-galactopyranoside as substrate. Maximum lactulose yields of 43% related to the initial lactose concentration are reached. The corresponding productivities are 52 g lactulose per l and h using Amberlite IRA-93 and 15 g lactulose per l and h unsing Eupergit C, respectively. While both carrier-bound CelB preparations are 100% stable for at least 14 days, the half-life of the free CelB in the enzyme membrane reactor is only about 1.5 days
synthesis
development of a microstructured immobilized enzyme reactor for production of beta-glucosylglycerol, transglycosylation reaction, under conditions of continuous flow at 70°C. CelB is covalently attached onto coated microchannel walls to give an effective enzyme activity of 30 U per total reactor working volume of 25 ml. Glycerol causes a concentration-dependent decrease in the conversion of the glucosyl donors 2-nitrophenyl beta-D-glucoside and cellobiose via hydrolysis and strongly suppresses participation of the substrate in the reaction as glucosyl acceptor. The yields of beta-glucosylglycerol are about 80% and 60% based on 2-nitrophenyl beta-D-glucoside and cellobiose converted, respectively, and maintain up to near exhaustion of substrate, giving about 120 mM (30 g/l) of beta-glucosylglycerol from the reaction of cellobiose and 1 M glycerol. The structure of the transglucosylation products is 1-O-beta-D-glucopyranosyl-rac-glycerol (79%) and 2-O-beta-D-glucopyranosyl-sn-glycerol (21%)
synthesis
expression of CleB gene in Escherichia coli gives approx 100000 U of enzyme activity/l of culture medium after 8 h of growth
synthesis
expression of enzyme using a baculovirus expression vector system in silkworm, Bombyx mori and purification to about 81% homogeneity in a single heat-treatment step. The expressed beta-glucosidase accounts for more than 10% of silkworm total haemolymph proteins. The expression level reaches 10199.5 U per ml hemolymph and 19797.4 U per silkworm larva, and the specific activity of the one-step purified crude enzyme is 885 U per mg
synthesis
hydrolysis of lactose in UHT skim milk at 70°C using CelB covalently attached onto Eupergit C in yields of 80%, and in a packed-bed immobilized enzyme reactor. The packed-bed reactor is about 10fold more stable and gives about the same productivity at 80% substrate conversion as the hollow-fiber reactor at 60% substrate conversion. The marked difference in the stability of free and immobilized CelB seems to reflect mainly binding of the soluble enzyme to the membrane surface of the hollow-fiber module. Microbial contamination of the reactors did not occur during reaction times of up to 39 d
synthesis
improvement of the stability of recombinant CelB by entrapment into Escherichia coli cells under conditions promoting strong inactivation. Glutardialdehyde-mediated protein cross-linking or rigidification of the cell membrane by adding magnesium ions is required to prevent release of CelB from within the cell into the bulk solution. In the presence of 1M glucose or when applying recirculation rates of 2.6per min, the entrapped enzyme is around 2fold more stable at 80°C than free CelB. The significance of the stabilisation is attenuated by the decrease in CelB initial activity which wis due to cross-linking and glutardialdehyde concentration-dependent
synthesis
use of CelB for oligosaccharide production from lactose in a kinetically controlled reaction. At reaction temperatures of 80°C and higher, the inactivation rate of the enzyme in the presence of sugars is increased by a factor of 2, caused by the occurrence of Maillard reactions between the sugar and the enzyme
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Comparative structural analysis and substrate specificity engineering of the hyperthermostable beta-glucosidase CelB from Pyrococcus furiosus
Biochemistry
39
4963-4970
2000
Pyrococcus furiosus (Q51723)
brenda
Kaper, T.; van Heusden, H.H.; van Loo, B.; Vasella, A.; van der Oost, J.; de Vos, W.M.
Substrate specificity engineering of beta-mannosidase and beta-glucosidase from Pyrococcus by exchange of unique active site residues
Biochemistry
41
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2002
Pyrococcus furiosus (Q51723)
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Bhmer, N.; Lutz-Wahl, S.; Fischer, L.
Recombinant production of hyperthermostable CelB from Pyrococcus furiosus in Lactobacillus sp.
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96
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2012
Pyrococcus furiosus (Q51723)
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Hansson, T.; Adlercreutz, P.
Enhanced transglucosylation/hydrolysis ratio of mutants of Pyrococcus furiosus beta-glucosidase: effects of donor concentration, water content, and temperature on activity and selectivity in hexanol
Biotechnol. Bioeng.
75
656-665
2001
Pyrococcus furiosus (Q51723)
brenda
Lang, M.; Kamrat, T.; Nidetzky, B.
Influence of ionic liquid cosolvent on transgalactosylation reactions catalyzed by thermostable beta-glycosylhydrolase CelB from Pyrococcus furiosus
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95
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Pyrococcus furiosus (Q51723)
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Quercetin production from rutin by a thermostable beta-rutinosidase from Pyrococcus furiosus
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Pyrococcus furiosus (Q51723)
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Kengen, S.W.; Luesink, E.J.; Stams, A.J.; Zehnder, A.J.
Purification and characterization of an extremely thermostable beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus
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1993
Pyrococcus furiosus
brenda
Petzelbauer, I.; Reiter, A.; Splechtna, B.; Kosma, P.; Nidetzky, B.
Transgalactosylation by thermostable beta-glycosidases from Pyrococcus furiosus and Sulfolobus solfataricus. Binding interactions of nucleophiles with the galactosylated enzyme intermediate make major contributions to the formation of new beta-glycosides
Eur. J. Biochem.
267
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2000
Pyrococcus furiosus (Q51723)
brenda
Pouwels, J.; Moracci, M.; Cobucci-Ponzano, B.; Perugino, G.; van der Oost, J.; Kaper, T.; Lebbink, J.H.; de Vos, W.M.; Ciaramella, M.; Rossi, M.
Activity and stability of hyperthermophilic enzymes: a comparative study on two archaeal beta-glycosidases
Extremophiles
4
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2000
Pyrococcus furiosus (Q51723)
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Yeom, S.J.; Kim, B.N.; Kim, Y.S.; Oh, D.K.
Hydrolysis of isoflavone glycosides by a thermostable beta-glucosidase from Pyrococcus furiosus
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60
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2012
Pyrococcus furiosus (Q51723)
brenda
Voorhorst, W.G.; Eggen, R.I.; Luesink, E.J.; de Vos, W.M.
Characterization of the celB gene coding for beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus and its expression and site-directed mutation in Escherichia coli
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177
7105-7111
1995
Pyrococcus furiosus (Q51723)
brenda
Park, S.H.; Park, K.H.; Oh, B.C.; Alli, I.; Lee, B.H.
Expression and characterization of an extremely thermostable beta-glycosidase (mannosidase) from the hyperthermophilic archaeon Pyrococcus furiosus DSM3638
N. Biotechnol.
28
639-648
2011
Pyrococcus furiosus (Q8U3U9)
brenda
Park, S.; Alli, I.; Park, K.; Oh, B.; Lee, B.
Mutation studies in the active site of beta-glycosidase from Pyrococcus furiosus DSM 3638
Protein Pept. Lett.
20
107-114
2013
Pyrococcus furiosus (Q8U3U9)
brenda
Hansson, T.; Adlercreutz, P.
Enzymatic synthesis of hexyl glycosides from lactose at low water activity and high temperature using hyperthermostable beta-glycosidases
Biocatal. Biotransform.
20
167-178
2002
Pyrococcus furiosus (Q51723)
-
brenda
Kaper, T.; Brouns, S.J.; Geerling, A.C.; De Vos, W.M.; Van der Oost, J.
DNA family shuffling of hyperthermostable beta-glycosidases
Biochem. J.
368
461-470
2002
Pyrococcus furiosus (Q51723)
brenda
Petzelbauer, I.; Nidetzky, B.; Haltrich, D.; Kulbe, K.D.
Development of an ultra-high-temperature process for the enzymatic hydrolysis of lactose. I. The properties of two thermostable beta-glycosidases
Biotechnol. Bioeng.
64
322-332
1999
Pyrococcus furiosus (Q51723)
brenda
Petzelbauer, I.; Splechtna, B.; Nidetzky, B.
Development of an ultrahigh-temperature process for the enzymatic hydrolysis of lactose. III. Utilization of two thermostable beta-glycosidases in a continuous ultrafiltration membrane reactor and galacto-oligosaccharide formation under steady-state conditions
Biotechnol. Bioeng.
77
394-404
2002
Pyrococcus furiosus (Q51723)
brenda
Petzelbauer, I.; Kuhn, B.; Splechtna, B.; Kulbe, K.D.; Nidetzky, B.
Development of an ultrahigh-temperature process for the enzymatic hydrolysis of lactose. IV. Immobilization of two thermostable beta-glycosidases and optimization of a packed-bed reactor for lactose conversion
Biotechnol. Bioeng.
77
619-631
2002
Pyrococcus furiosus
brenda
Hansson, T.; Adlercreutz, P.
The temperature influences the ratio of glucosidase and galactosidase activities of beta-glycosidases
Biotechnol. Lett.
24
1465-1471
2002
Pyrococcus furiosus (Q51723)
-
brenda
Hansson, T.; Andersson, M.; Wehtje, E.; Adlercreutz, P.
Influence of water activity on the competition between beta-glycosidase-catalysed transglycosylation and hydrolysis in aqueous hexanol
Enzyme Microb. Technol.
29
527-534
2001
Pyrococcus furiosus (Q51723)
-
brenda
Shin, K.C.; Nam, H.K.; Oh, D.K.
Hydrolysis of flavanone glycosides by beta-glucosidase from Pyrococcus furiosus and its application to the production of flavanone aglycones from citrus extracts.
J. Agric. Food Chem.
61
11532-11540
2013
Pyrococcus furiosus (Q51723)
brenda
Nakabayashi, M.; Kataoka, M.; Watanabe, M.; Ishikawa, K.
Monomer structure of a hyperthermophilic beta-glucosidase mutant forming a dodecameric structure in the crystal form
Acta Crystallogr. Sect. F
70
854-859
2014
Pyrococcus furiosus (Q51723)
brenda
Kado, Y.; Inoue, T.; Ishikawa, K.
Structure of hyperthermophilic beta-glucosidase from Pyrococcus furiosus
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67
1473-1479
2011
Pyrococcus furiosus (Q51723)
brenda
Splechtna, B.; Petzelbauer, I.; Kuhn, B.; Kulbe, K.D.; Nidetzky, B.
Hydrolysis of lactose by beta-glycosidase CelB from hyperthermophilic archaeon Pyrococcus furiosus: comparison of hollow-fiber membrane and packed-bed immobilized enzyme reactors for continuous processing of ultrahigh temperature-treated skim milk
Appl. Biochem. Biotechnol.
98-100
473-88
2002
Pyrococcus furiosus (Q51723)
brenda
Yoo, M.H.; Yeom, S.J.; Park, C.S.; Lee, K.W.; Oh, D.K.
Production of aglycon protopanaxadiol via compound K by a thermostable beta-glycosidase from Pyrococcus furiosus
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89
1019-1028
2011
Pyrococcus furiosus (Q51723)
brenda
Lebbink, J.H.; Kaper, T.; Bron, P.; van der Oost, J.; de Vos, W.M.
Improving low-temperature catalysis in the hyperthermostable Pyrococcus furiosus beta-glucosidase CelB by directed evolution
Biochemistry
39
3656-3665
2000
Pyrococcus furiosus (Q51723)
brenda
Perugino, G.; Trincone, A.; Giordano, A.; van der Oost, J.; Kaper, T.; Rossi, M.; Moracci, M.
Activity of hyperthermophilic glycosynthases is significantly enhanced at acidic pH
Biochemistry
42
8484-8493
2003
Pyrococcus furiosus (Q51723)
brenda
Schwarz, A.; Thomsen, M.S.; Nidetzky, B.
Enzymatic synthesis of beta-glucosylglycerol using a continuous-flow microreactor containing thermostable beta-glycoside hydrolase CelB immobilized on coated microchannel walls
Biotechnol. Bioeng.
103
865-872
2009
Pyrococcus furiosus (Q51723)
brenda
Bruins, M.E.; Van Hellemond, E.W.; Janssen, A.E.; Boom, R.M.
Maillard reactions and increased enzyme inactivation during oligosaccharide synthesis by a hyperthermophilic glycosidase
Biotechnol. Bioeng.
81
546-552
2003
Pyrococcus furiosus (Q51723), Pyrococcus furiosus
brenda
Watanabe,M.; Fujiwara, M.; Ishikawa, K.
Encapsulation of hyperthermophilic beta-glucosidase from Pyrococcus furiosus into silica microcapsules
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43
1272-1274
2014
Pyrococcus furiosus (Q51723)
-
brenda
Powers, S.L.; Robinson, C.R.; Robinson, A.S.
Denaturation of an extremely stable hyperthermophilic protein occurs via a dimeric intermediate
Extremophiles
11
179-189
2007
Pyrococcus furiosus (Q51723)
brenda
Voorhorst, W.G.B.; Gueguen, Y.; Geerling, A.C.M.; Schut, G.; Dahlke, I.; Thomm, M.; van der Oost, J.; de Vos, W.M.
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181
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1999
Pyrococcus furiosus (Q51723)
brenda
Kamrat, T.; Nidetzky, B.
Entrapment in E. coli improves the operational stability of recombinant beta-glycosidase CelB from Pyrococcus furiosus and facilitates biocatalyst recovery
J. Biotechnol.
129
69-76
2007
Pyrococcus furiosus (Q51723)
brenda
Mayer, J.; Kranz, B.; Fischer, L.
Continuous production of lactulose by immobilized thermostable beta-glycosidase from Pyrococcus furiosus
J. Biotechnol.
145
387-393
2010
Pyrococcus furiosus (Q51723)
brenda
Bruins, M.E.; Janssen, A.E.M.; Boom, R.M.
Equilibrium shifts in enzyme reactions at high pressure
J. Mol. Catal. B
39
124-127
2006
Pyrococcus furiosus (Q51723)
-
brenda
Zeuner, B.; Nyffenegger, C.; Mikkelsen, J.D.; Meyer, A.S.
Thermostable beta-galactosidases for the synthesis of human milk oligosaccharides
N. Biotechnol.
33
355-60
2016
Pyrococcus furiosus (Q51723)
brenda
Lin, X.A.; Zhang, W.; Chen, Y.; Yao, B.; Zhang, Z.F.
Overexpression of celB gene coding for beta-glucosidase from Pyrococcus furiosus using a baculovirus expression vector system in silkworm, Bombyx mori
Z. Naturforsch. C
61
595-600
2006
Pyrococcus furiosus (Q51723)
brenda
Choi, J.H.; Shin, K.C.; Oh, D.K.
An L213A variant of beta-glycosidase from Sulfolobus solfataricus with increased alpha-L-arabinofuranosidase activity converts ginsenoside Rc to compound K
PLoS ONE
13
e0191018
2018
Pyrococcus furiosus
brenda
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