Any feedback?
Information on EC 3.2.1.192 - ginsenoside Rb1 beta-glucosidase
for references in articles please use BRENDA:EC3.2.1.192Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
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, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BGL3T
bgp1C
GH3 beta-glucosidase
ginsenoside Rb1-converting enzyme
Theth_1706
Tpebgl3
Tpet_0898
Tt-BGL
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no significant effect of 5 mM EDTA on the enzyme activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
121
4-nitrophenyl beta-D-glucopyranoside
pH 5.0, 90°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
90
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT