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Information on EC 3.2.1.192 - ginsenoside Rb1 beta-glucosidase
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3.2.1.192 ginsenoside Rb1 beta-glucosidaseIUBMB Comments
Ginsenosidases catalyse the hydrolysis of glycosyl moieties attached to the C-3, C-6 or C-20 position of ginsenosides. They are specific with respect to the nature of the glycosidic linkage, the position and the order in which the linkages are cleaved. Ginsenoside Rb1 beta-glucosidase specifically and sequentially hydrolyses the 20-[beta-D-glucopyranosyl-(1->6)-beta-D glucopyranosyloxy] residues attached to position 20 by first hydrolysing the (1->6)-glucosidic bond to generate ginsenoside Rd as an intermediate, followed by hydrolysis of the remaining 20-O-beta-D-glucosidic bond.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
BGL3T, bgp1, bgp1C, GH3 beta-glucosidase, ginsenoside Rb1-converting enzyme, More, Theth_1706, Tpebgl3, Tpet_0898, Tt-BGL, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BGL3T
bgp1C
GH3 beta-glucosidase
ginsenoside Rb1-converting enzyme
Theth_1706
Tpebgl3
Tpet_0898
Tt-BGL
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ginsenoside Rb1 + H2O = ginsenoside Rd + D-glucopyranose
-
-
-
-
ginsenoside Rd + H2O = ginsenoside Rg3 + D-glucopyranose
-
-
-
-
ginsenoside Rb1 + 2 H2O = ginsenoside Rg3 + 2 D-glucopyranose
overall reaction
-
ginsenoside Rb1 + 2 H2O = ginsenoside Rg3 + 2 D-glucopyranose
overall reaction
-
-
ginsenoside Rb1 + 2 H2O = ginsenoside Rg3 + 2 D-glucopyranose
overall reaction
Paecilomyces sp. (in: Eurotiomycetes) 220 Bainier
-
-
ginsenoside Rb1 + 2 H2O = ginsenoside Rg3 + 2 D-glucopyranose
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
ginsenoside Rb1 glucohydrolase
Ginsenosidases catalyse the hydrolysis of glycosyl moieties attached to the C-3, C-6 or C-20 position of ginsenosides. They are specific with respect to the nature of the glycosidic linkage, the position and the order in which the linkages are cleaved. Ginsenoside Rb1 beta-glucosidase specifically and sequentially hydrolyses the 20-[beta-D-glucopyranosyl-(1->6)-beta-D glucopyranosyloxy] residues attached to position 20 by first hydrolysing the (1->6)-glucosidic bond to generate ginsenoside Rd as an intermediate, followed by hydrolysis of the remaining 20-O-beta-D-glucosidic bond.
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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-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
-
-
-
-
?
2-nitrophenyl-beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucopyranose
-
no hydrolysis of 4-nitrophenyl-alpha-D-glucoside or 4-nitrophenyl-beta-D-xyloside
-
-
?
4-nitrophenyl-beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
-
?
ginsenoside F1 + H2O
protopanaxatriol + D-glucose
reaction of EC 3.2.1.194
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rg3 + 2 D-glucose
-
-
-
?
ginsenoside Re + H2O
ginsenoside Rg2 + L-rhamnose
reaction of EC 3.2.1.194
-
-
?
ginsenoside Rg1 + H2O
ginsenoside Rh1 + D-glucose
reaction of EC 3.2.1.194
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucopyranose
low activity
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucopyranose
low activity
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucopyranose
low activity
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucopyranose
low activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
Aspergillus versicolor LFJ1403
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
Pseudothermotoga thermarum DSM 5069 T
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
?
ginsenoside compound K + H2O
20(S)-protopanaxadiol + D-glucopyranose
33% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
ginsenoside compound K + H2O
20(S)-protopanaxadiol + D-glucopyranose
35% activity compared to ginsenoside Rb1
-
-
?
ginsenoside F2 + H2O
ginsenoside 20(S)-Rh2 + D-glucopyranose
34% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
ginsenoside F2 + H2O
ginsenoside 20(S)-Rh2 + D-glucopyranose
91% activity compared to ginsenoside Rb1
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
-
-
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
-
-
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
-
hydrolysis of 20-O-beta-D-glucosyl-beta-D-(1->6)-glucosidic bond
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
-
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
118% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
Pseudothermotoga thermarum DSM 5069 T
-
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
Pseudothermotoga thermarum DSM 5069 T
118% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
best ginsenoside substrate
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
-
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
best ginsenoside substrate
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
-
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
best ginsenoside substrate
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
-
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
best ginsenoside substrate
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rg3 + D-glucopyranose
direct conversion of Rb1 into Rg3
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rg3 + D-glucopyranose
direct conversion of Rb1 into Rg3
-
-
?
ginsenoside Rd + H2O
ginsenoside 20(S)-Rg3 + D-glucopyranose
43% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
ginsenoside Rd + H2O
ginsenoside 20(S)-Rg3 + D-glucopyranose
84% activity compared to ginsenoside Rb1
-
-
?
ginsenoside Rd + H2O
ginsenoside Rg3 + D-glucopyranose
-
hydrolyzes the 20-O-glucoside of Rd at 44% of the activity compared to the hydrolysis of the 20-O-beta-D-glucosyl-beta-D-(1->6)-glucosidic bond of ginsenoside Rb1
-
-
?
ginsenoside Rd + H2O
ginsenoside Rg3 + D-glucopyranose
-
-
-
?
ginsenoside Rd + H2O
ginsenoside Rg3 + D-glucopyranose
Pseudothermotoga thermarum DSM 5069 T
-
-
-
?
ginsenoside Rd + H2O
ginsenoside Rg3 + D-glucopyranose
-
-
-
?
ginsenoside Rd + H2O
ginsenoside Rg3 + D-glucopyranose
-
-
-
?
ginsenoside Rd + H2O
ginsenoside Rg3 + D-glucopyranose
-
-
-
?
ginsenoside Rd + H2O
ginsenoside Rg3 + D-glucose
-
-
-
?
ginsenoside Re + H2O
ginsenoside Rg2 + D-glucopyranose
110% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
ginsenoside Re + H2O
ginsenoside Rg2 + D-glucopyranose
81% activity compared to ginsenoside Rb1
-
-
?
ginsenoside Rg1 + H2O
ginsenoside 20(S)-Rh1 + D-glucopyranose
81% activity compared to 4-nitrophenyl beta-D-glucopyranoside
-
-
?
ginsenoside Rg1 + H2O
ginsenoside 20(S)-Rh1 + D-glucopyranose
64% activity compared to ginsenoside Rb1
-
-
?
additional information
?
-
-
beta-galactosidase from Aspergillus sp. displays beta-glucosidase activity, which is responsible for its ability to transform major ginsenoside Rb1 to rare ginsenoside F2 and to ginsenoside Rg3 via ginsenoside Rd. Ginsenoside Rg3 can be selectively hydrolyzed and only Rh2 is obtained with this beta-galactosidase. Before hydrolysis, an Rg3 inclusion complex is prepared with hydroxypropyl-b-cyclodextrin (HP-beta-CD) to improve the aqueous solubility. The solubility of Rg3 increases 74.6fold, and the phase solubility curve displays a typical AL-type, which indicates the formation of a 1:1 inclusion complex. Using an enzyme loading of 500 U/g Rg3, the highest Rg3 conversion of 90.6% and Rh2 yield of 88.5% are obtained after 24 h at 60°C. Ginsenoside F2 is not converted into ginsenoside Rh2 and this is not converted into the protopanaxadiol aglycone
-
-
?
additional information
?
-
Burkholderia sp. GE 17-7
-
substrate and product analysis by thin layer chromatography and 13C-NMR spectroscopy. Maximum conversion rate of ginsenoside Rb1 to Rg3 is 98%
-
-
?
additional information
?
-
-
substrate specificity of beta-glucosidase from Gordonia terrae for ginsenosides, overview. The purified recombinant enzyme specifically hydrolyzes the glucopyranosides at the C-20 position in protopanaxadiol (PPD)-type ginsenosides and hydrolyzes the glucopyranoside at the C-6 or C-20 position in protopanaxatriol (PPT)-type ginsenosides. The enzyme is a beta-glucosidase with xylopyranoside-hydrolyzing activity that is active with 4-nitrophenyl-beta-D-xylopyranoside and 2-nitrophenyl-beta-D-xylopyranoside. The specific activity for PPD-type ginsenosides as substrates is in the order gypenoside XVII > gypenoside LXXV > Rb1 > F2 > compound K > Rd, and the products are F2, compound K, Rd, Rh2, APPD, and Rg3, respectively. The specific activity for PPT-type ginsenosides as substrates follows the order F1 > Re > Rg1 > notoginsenoside R1 > Rh1 and the products of which are APPT, Rg2, Rh1, notoginsenoside R2, and APPT, respectively. No activity with ginsenosides Rb2, Rc, Compound Mc, Compound Mc-1, Compound O, and Compound Y, as well as with notoginsenoside R2 and ginsenoside Rg2. No activity is found for 4-nitrophenyl-alpha-D-glucopyranoside, 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-alpha-D-galactopyranoside, 4-nitrophenyl-alpha-L-arabinofuranose, 4-nitrophenyl-alpha-L-arabinopyranose, or 4-nitrophenyl-alpha-L-rhamnopyranoside
-
-
?
additional information
?
-
the recombinant beta-glucosidase enzyme (bgp1) hydrolyzes all glucose moieties attached to the C-20 position of the ginsenosides Rg1, Re, Rb1, Rd, and F1. The products include pharmacologically active minor ginsenosides Rh1, Rg2, Rg3, F1, and protopanaxatriol. TLC and HPLC analysis of ginsenoside transformation by enzyme bgp1, overview
-
-
?
additional information
?
-
-
no hydrolysis of the 20-O-alpha-D-(1->6)-arabinopyranosidic bond of ginsenoside Rb2 and the 20-O-beta-D-(1->6)-xylosidic bond of ginsenoside Rb3. It does not hydrolyse the 3-O-beta-glucosidic bond of ginsenoside Rb1, Rb2, Rb3
-
-
?
additional information
?
-
the beta-glucosidase exhibits high selectivity to cleave the outer and inner glucopyranosyl moieties at the C-20 carbon of ginsenoside Rb1 and catalyzes the conversion of ginsenoside Rb1 or Rd to the more pharmacologically active minor ginsenoside 20(S)-Rg3. The enzyme is also able to hydrolyze cellobiose and gentiobiose. No activity is detected with 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-beta-D-xylopyranoside, 4-nitrophenyl-alpha-L-arabinofuranoside, carboxymethyl cellulose, and sucrose
-
-
?
additional information
?
-
Pseudothermotoga thermarum DSM 5069 T
the beta-glucosidase exhibits high selectivity to cleave the outer and inner glucopyranosyl moieties at the C-20 carbon of ginsenoside Rb1 and catalyzes the conversion of ginsenoside Rb1 or Rd to the more pharmacologically active minor ginsenoside 20(S)-Rg3. The enzyme is also able to hydrolyze cellobiose and gentiobiose. No activity is detected with 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-beta-D-xylopyranoside, 4-nitrophenyl-alpha-L-arabinofuranoside, carboxymethyl cellulose, and sucrose
-
-
?
additional information
?
-
the beta-glucosidase shows preference for cleaving the outer and inner glucopyranosyl moieties at the C-20 carbon of ginsenoside Rb1, which produces the pharmacologically active minor ginsenoside 20(S)-Rg3, via graded hydrolysis of the two glucoses at C-20 or direct hydrolysis of the inner glucoses at C-20. The ginsenoside Rg3 exists as two optical isomers, ginsenoside 20(S)-Rg3 and 20(R)-Rg3. The 20(S)-Rg3 isomer is superior to the 20(R)-Rg3 isomer in terms of its water solubility and bioavailability because of the spatial arrangement of the hydroxyl group on carbon 20. No or poor activity with ginsenosides Rb2, Rc, (S)-Rh2, (S)-Rg3, Rg2, and (S)-Rh1 as substrates, no activity with 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-alpha--L-arabinofuranoside, 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-alpha-L-rhamnopyranoside, 4-nitrophenyl-beta-D-xylopyranoside. Low activity with gentiobiose and cellobiose. No activity with laminaribiose and sucrose. The enzyme also has broadly specific beta-glucosidase activity against a wide range of substrates with different glycosidic bonds, including aryl-beta-glucosidic bonds and alkyl-beta-glucosidic bonds, and oligosaccharides
-
-
?
additional information
?
-
the beta-glucosidase shows preference for cleaving the outer and inner glucopyranosyl moieties at the C-20 carbon of ginsenoside Rb1, which produces the pharmacologically active minor ginsenoside 20(S)-Rg3, via graded hydrolysis of the two glucoses at C-20 or direct hydrolysis of the inner glucoses at C-20. The ginsenoside Rg3 exists as two optical isomers, ginsenoside 20(S)-Rg3 and 20(R)-Rg3. The 20(S)-Rg3 isomer is superior to the 20(R)-Rg3 isomer in terms of its water solubility and bioavailability because of the spatial arrangement of the hydroxyl group on carbon 20. No or poor activity with ginsenosides Rb2, Rc, (S)-Rh2, (S)-Rg3, Rg2, and (S)-Rh1 as substrates, no activity with 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-alpha--L-arabinofuranoside, 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-alpha-L-rhamnopyranoside, 4-nitrophenyl-beta-D-xylopyranoside. Low activity with gentiobiose and cellobiose. No activity with laminaribiose and sucrose. The enzyme also has broadly specific beta-glucosidase activity against a wide range of substrates with different glycosidic bonds, including aryl-beta-glucosidic bonds and alkyl-beta-glucosidic bonds, and oligosaccharides
-
-
?
additional information
?
-
the beta-glucosidase shows preference for cleaving the outer and inner glucopyranosyl moieties at the C-20 carbon of ginsenoside Rb1, which produces the pharmacologically active minor ginsenoside 20(S)-Rg3, via graded hydrolysis of the two glucoses at C-20 or direct hydrolysis of the inner glucoses at C-20. The ginsenoside Rg3 exists as two optical isomers, ginsenoside 20(S)-Rg3 and 20(R)-Rg3. The 20(S)-Rg3 isomer is superior to the 20(R)-Rg3 isomer in terms of its water solubility and bioavailability because of the spatial arrangement of the hydroxyl group on carbon 20. No or poor activity with ginsenosides Rb2, Rc, (S)-Rh2, (S)-Rg3, Rg2, and (S)-Rh1 as substrates, no activity with 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-alpha--L-arabinofuranoside, 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-alpha-L-rhamnopyranoside, 4-nitrophenyl-beta-D-xylopyranoside. Low activity with gentiobiose and cellobiose. No activity with laminaribiose and sucrose. The enzyme also has broadly specific beta-glucosidase activity against a wide range of substrates with different glycosidic bonds, including aryl-beta-glucosidic bonds and alkyl-beta-glucosidic bonds, and oligosaccharides
-
-
?
additional information
?
-
the beta-glucosidase shows preference for cleaving the outer and inner glucopyranosyl moieties at the C-20 carbon of ginsenoside Rb1, which produces the pharmacologically active minor ginsenoside 20(S)-Rg3, via graded hydrolysis of the two glucoses at C-20 or direct hydrolysis of the inner glucoses at C-20. The ginsenoside Rg3 exists as two optical isomers, ginsenoside 20(S)-Rg3 and 20(R)-Rg3. The 20(S)-Rg3 isomer is superior to the 20(R)-Rg3 isomer in terms of its water solubility and bioavailability because of the spatial arrangement of the hydroxyl group on carbon 20. No or poor activity with ginsenosides Rb2, Rc, (S)-Rh2, (S)-Rg3, Rg2, and (S)-Rh1 as substrates, no activity with 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-alpha--L-arabinofuranoside, 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-alpha-L-rhamnopyranoside, 4-nitrophenyl-beta-D-xylopyranoside. Low activity with gentiobiose and cellobiose. No activity with laminaribiose and sucrose. The enzyme also has broadly specific beta-glucosidase activity against a wide range of substrates with different glycosidic bonds, including aryl-beta-glucosidic bonds and alkyl-beta-glucosidic bonds, and oligosaccharides
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
ginsenoside F1 + H2O
protopanaxatriol + D-glucose
reaction of EC 3.2.1.194
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rg3 + 2 D-glucose
-
-
-
?
ginsenoside Re + H2O
ginsenoside Rg2 + L-rhamnose
reaction of EC 3.2.1.194
-
-
?
ginsenoside Rg1 + H2O
ginsenoside Rh1 + D-glucose
reaction of EC 3.2.1.194
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
-
-
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
-
-
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
-
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
Pseudothermotoga thermarum DSM 5069 T
-
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
-
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
-
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucopyranose
-
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rg3 + D-glucopyranose
direct conversion of Rb1 into Rg3
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rg3 + D-glucopyranose
direct conversion of Rb1 into Rg3
-
-
?
ginsenoside Rd + H2O
ginsenoside Rg3 + D-glucopyranose
-
-
-
?
ginsenoside Rd + H2O
ginsenoside Rg3 + D-glucopyranose
Pseudothermotoga thermarum DSM 5069 T
-
-
-
?
ginsenoside Rd + H2O
ginsenoside Rg3 + D-glucopyranose
-
-
-
?
ginsenoside Rd + H2O
ginsenoside Rg3 + D-glucopyranose
-
-
-
?
ginsenoside Rd + H2O
ginsenoside Rg3 + D-glucopyranose
-
-
-
?
ginsenoside Rd + H2O
ginsenoside Rg3 + D-glucose
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
activates about 1.5fold at 5 mM, stabilizes the purified recombinant enzyme
Co2+
activates about 1.5fold at 5 mM, does not stabilize the purified recombinant enzyme
Mn2+
activates about 1.5fold at 5 mM, stabilizes the purified recombinant enzyme
additional information
no or poor effects by 1 mM of Ni2+, Fe3+, Mg2+, Zn2+, K+, Ca2+, Li+, and Co2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no significant effect of 5 mM EDTA on the enzyme activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.065
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, recombinant enzyme
14.66
4-nitrophenyl-beta-D-glucopyranoside
-
recombinant enzyme, pH 6.5, 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
121
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, recombinant enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1861
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, recombinant enzyme
1057.7
4-nitrophenyl-beta-D-glucopyranoside
-
recombinant enzyme, pH 6.5, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70.7
purified recombinant His-tagged enzyme, pH 5.0, 90°C, substrate is 4-nitrophenyl beta-D-glucopyranoside
95.7
purified recombinant His-tagged enzyme, pH 5.0, 90°C, substrate is 4-nitrophenyl beta-D-glucopyranoside
additional information
additional information
Paenibacillus sp. MBT213
-
crude enzyme of strain MBT213 exhibits high conversion capacity on ginsenoside Rb1 into ginsenoside Rd, under optimal conditions for 14 days, 3.794 mg/ml of ginsenoside Rb1 is fully hydrolyzed by crude enzyme of strain MBT213
additional information
at a concentration of 0.75 U/mL of the enzyme, a temperature of 85°C and pH 5.0,10 g/l ginsenoside Rb1 is transformed into 6.9 g/l Rg3 within 60 min with a corresponding molar conversion of 97.8%
additional information
in a reaction at 90°C and pH 5.0, 10 g/l of ginsenoside Rb1 is transformed into 6.93 g/l of Rg3 within 90 min, with a corresponding molar conversion of 97.9 %, and Rg3 productivity of 4620 mg/l/h
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 5
-
pH 2.5: about 45% of maximal activity, pH 5.0: about 45% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
90
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 60
-
40°C: about 50% of maximal activity. 60°C: about 60% of maximal activity
65 - 100
activity profile of the recombinant enzyme, overview
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Burkholderia sp. GE 17-7
isolated from Panax ginseng collected from Ji-an City (Jilin, China), endophytic bacterium
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
enzyme production of ginsenoside Rd is highest at pH 5.0, 37°C, compariosn of enzyme activities in different biotransformation systems within 96 h, overview
brenda
Aspergillus versicolor LFJ1403
-
enzyme production of ginsenoside Rd is highest at pH 5.0, 37°C, compariosn of enzyme activities in different biotransformation systems within 96 h, overview
-
brenda
additional information
-
at pH 6.0, 40°C, and 2% w/v cellobiose beta-glucosidase production in Lactobacillus rhamnosus strain GG is enhanced by 25fold, optimization of microbial media composition for production of beta-glucosidase from strain GG, overview
brenda
additional information
-
at pH 6.0, 40°C, and 2% w/v cellobiose beta-glucosidase production in Lactobacillus rhamnosus strain GG is enhanced by 25fold, optimization of microbial media composition for production of beta-glucosidase from strain GG, overview
-
brenda
additional information
Paenibacillus sp. MBT213
-
crude enzyme of strain MBT213 exhibits high conversion capacity on ginsenoside Rb1 into ginsenoside Rd. After 10 days of optimal reaction conditions for the crude enzyme, ginsenoside Rb1 is fully converted to ginsenoside Rd
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
strain LFJ1403 secretes ginsenoside-converting enzymes in the spore production phase of plate culture
-
brenda
Aspergillus versicolor LFJ1403
-
strain LFJ1403 secretes ginsenoside-converting enzymes in the spore production phase of plate culture
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
Paenibacillus sp. MBT213
-
ginsenoside Rd is the main hydrolyzed product of ginsenoside Rb1, Rb2, and Rc, which are contained more than 80% in ginseng roots. Also ginsenoside Rd is the major precursor of ginsenoside Rg3, Rh2, F2 and compound K, which have high biological activities
evolution
the enzyme belongs to the glycosyl hydrolase family 3, GH3
evolution
the enzyme belongs to the glycosyl hydrolase family 3, GH3. Alignment of the Tpebgl3 cluster with several GH3 beta-glucosidases indicates that they share some conserved motifs: CIHKFV (residues 162-167), GFVMSDWYAGDN (residues 238-249) and IVISRISGEGYDRK (residues 452-463)
evolution
-
the enzyme belongs to the glycosyl hydrolase family 3, GH3. Alignment of the Tpebgl3 cluster with several GH3 beta-glucosidases indicates that they share some conserved motifs: CIHKFV (residues 162-167), GFVMSDWYAGDN (residues 238-249) and IVISRISGEGYDRK (residues 452-463)
-
evolution
Pseudothermotoga thermarum DSM 5069 T
-
the enzyme belongs to the glycosyl hydrolase family 3, GH3
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 3, GH3. Alignment of the Tpebgl3 cluster with several GH3 beta-glucosidases indicates that they share some conserved motifs: CIHKFV (residues 162-167), GFVMSDWYAGDN (residues 238-249) and IVISRISGEGYDRK (residues 452-463)
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 3, GH3. Alignment of the Tpebgl3 cluster with several GH3 beta-glucosidases indicates that they share some conserved motifs: CIHKFV (residues 162-167), GFVMSDWYAGDN (residues 238-249) and IVISRISGEGYDRK (residues 452-463)
-
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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). A0A142G555_9MICO
500
0
52012
TrEMBL
-
A5IL43_THEP1
Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1)
722
0
81244
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
?
x * 81000, recombinant His-tagged enzyme, SDS-PAGE, x * 81243, sequence calculation
?
-
x * 81000, recombinant His-tagged enzyme, SDS-PAGE, x * 81243, sequence calculation
-
?
-
x * 81000, recombinant His-tagged enzyme, SDS-PAGE, x * 81243, sequence calculation
-
?
-
x * 81000, recombinant His-tagged enzyme, SDS-PAGE, x * 81243, sequence calculation
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 7.5
purified recombinant His-tagged enzyme, completely stable at pH 7.5, 50% activity at pH 3.5
754332
4.5 - 7.5
purified recombinant His-tagged enzyme, 80% activity remaining at pH 4.5-7.5
754434
5.5
purified recombinant His-tagged enzyme, completely stable at
754434
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
purified recombinant His-tagged enzyme, pH 5.0, about 90% activity remaining after 180 min
80
purified recombinant His-tagged enzyme, pH 5.0, about 70% activity remaining after 180 min
85
purified recombinant His-tagged enzyme, pH 5.0, about 90% activity remaining after 120 min
90
95
purified recombinant His-tagged enzyme, pH 5.0, about 10% activity remaining after 120 min, 20% after 60 min
90
purified recombinant His-tagged enzyme, pH 5.0, 50% activity remaining after 60 min, 40% after 120 min
90
purified recombinant His-tagged enzyme, pH 5.0, about 45% activity remaining after 180 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
whole-cell homogenates show the highest beta-glucosidase activity when compared with disrupted cell suspensions. The cell disruption step significantly decreases the beta-glucosidase activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
only two chromatographic steps, QSepharose FF and microcrystalline cellulose column in sequence, are required to purify the enzyme to homogeneity
-
recombinant His-tagged enzyme 2.9fold from Escherichia coli strain BL21(DE3) by heat treatment and nickel affinity chromatography
recombinant His-tagged enzyme 6.1fold from Escherichia coli strain BL21(DE3) by heat treatment and nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Theth_1706, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain JM109(DE3)
gene Tpet_0898, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) partly in inclusion bodies, method optimization
recombinant enzyme expression in Escherichia coli strain BL21(DE3)
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
2-5% cellobiose induce enzyme expression
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
industrial applications of Lactobacillus rhamnosus strain GG to the biocatalysis of ginsenosides and/or other phytochemicals
synthesis
-
the beta-galactosidase from Aspergillus sp. can be useful for the mass production of rare ginsenosides
synthesis
Paenibacillus sp. MBT213
-
the beta-glucosidase activity of Paenibacillus sp. MBT213 strain may be utilized in development of variety of health foods, dairy foods and pharmaceutical products
synthesis
-
industrial applications of Lactobacillus rhamnosus strain GG to the biocatalysis of ginsenosides and/or other phytochemicals
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yan, Q.; Zhou, W.; Li, X.; Feng, M.; Zhou, P.
Purification method improvement and characterization of a novel ginsenoside-hydrolyzing beta-glucosidase from Paecilomyces Bainier sp. 229
Biosci. Biotechnol. Biochem.
72
352-359
2008
Paecilomyces sp. (in: Eurotiomycetes), Paecilomyces sp. (in: Eurotiomycetes) 220 Bainier
brenda
Lin, F.; Guo, X.; Lu, W.
Efficient biotransformation of ginsenoside Rb1 to Rd by isolated Aspergillus versicolor, excreting beta-glucosidase in the spore production phase of solid culture
Antonie van Leeuwenhoek
108
1117-1127
2015
Aspergillus versicolor, Aspergillus versicolor LFJ1403
brenda
Huq, M.; Siraj, F.; Kim, Y.; Yang, D.
Enzymatic transformation of ginseng leaf saponin by recombinant beta-glucosidase (bgp1) and its efficacy in an adipocyte cell line
Biotechnol. Appl. Biochem.
63
532-538
2016
Microbacterium esteraromaticum (A0A142G555)
-
brenda
Fu, Y.; Yin, Z.H.; Yin, C.Y.
Biotransformation of ginsenoside Rb1 to ginsenoside Rg3 by endophytic bacterium Burkholderia sp. GE 17-7 isolated from Panax ginseng
J. Appl. Microbiol.
122
1579-1585
2017
Burkholderia sp. GE 17-7
brenda
Shin, K.; Lee, H.; Oh, D.
Substrate specificity of beta-glucosidase from Gordonia terrae for ginsenosides and its application in the production of ginsenosides Rg3, Rg2, and Rh1 from ginseng root extract
J. Biosci. Bioeng.
119
497-504
2015
Gordonia terrae, Gordonia terrae DSM 43249, Gordonia terrae NBRC 100016
brenda
Xie, J.; Zhao, D.; Zhao, L.; Pei, J.; Xiao, W.; Ding, G.; Wang, Z.
Overexpression and characterization of a Ca2+ activated thermostable beta-glucosidase with high ginsenoside Rb1 to ginsenoside 20(S)-Rg3 bioconversion productivity
J. Ind. Microbiol. Biotechnol.
42
839-850
2015
Thermotoga petrophila (A5IL43), Thermotoga petrophila DSM 13995 (A5IL43), Thermotoga petrophila RKU-1 (A5IL43), Thermotoga petrophila ATCC BAA-488 (A5IL43)
brenda
Ku, S.; You, H.J.; Park, M.S.; Ji, G.E.
Whole-cell biocatalysis for producing ginsenoside Rd from Rb1 using Lactobacillus rhamnosus GG
J. Microbiol. Biotechnol.
26
1206-1215
2016
Lacticaseibacillus rhamnosus, Lacticaseibacillus rhamnosus GG
brenda
Pei, J.; Xie, J.; Yin, R.; Zhao, L.; Ding, G.; Wang, Z.; Xiao, W.
Enzymatic transformation of ginsenoside Rb1 to ginsenoside 20(S)-Rg3 by GH3 beta-glucosidase from Thermotoga thermarum DSM 5069 T
J. Mol. Catal. B
113
104-109
2015
Pseudothermotoga thermarum (F7YVT1), Pseudothermotoga thermarum DSM 5069 T (F7YVT1)
-
brenda
Renchinkhand, G.; Cho, S.H.; Urgamal, M.; Park, Y.W.; Nam, J.H.; Bae, H.C.; Song, G.Y.; Nam, M.S.
Characterization of Paenibacillus sp. MBT213 isolated from raw milk and its ability to convert ginsenoside Rb1 into ginsenoside Rd from Panax ginseng
Korean J. Food Sci. Anim. Resour.
37
735-742
2017
Paenibacillus sp. MBT213
brenda
Wan, H.; Li, D.
Highly efficient biotransformation of ginsenoside Rb1 and Rg3 using beta-galactosidase from Aspergillus sp.
RSC Adv.
5
78874-78879
2015
Aspergillus sp.
-
brenda
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