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Information on EC 3.2.1.193 - ginsenosidase type I
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3.2.1.193 ginsenosidase type IIUBMB Comments
Ginsenosidase type I is slightly activated by Mg2+ or Ca2+ . The enzyme hydrolyses the 3-O-beta-D-(1->2)-glucosidic bond, the 3-O-beta-D-glucopyranosyl bond and the 20-O-beta-D-(1->6)-glycosidic bond of protopanaxadiol-type ginsenosides. It usually leaves a single glucosyl residue attached at position 20 and one or no glucosyl residues at position 3. Starting with a ginsenoside that is glycosylated at both positions (e.g. ginsenoside Rb1, Rb2, Rb3, Rc or Rd), the most common products are ginsenoside F2 and ginsenoside C-K, with low amounts of ginsenoside Rh2.
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Word Map
- 3.2.1.193
- ginseng
- aspergillus
- protopanaxadiol
- paecilomyces
-
bioreactor
- panax
- glycoside
- mucilaginosus
-
paenibacillus
- niger
- synthesis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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Synonyms
bglpm, ginsenoside-hydrolyzing beta-glucosidase, ginsenosidase type-i, ginsenosidase type i, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-glucosidase
BG-1
Bgl
BglPm
bgy2
ginsenosidase type I
ginsenosidase type-I
ginsenoside Rc-hydrolyzing beta-glucosidase
ginsenoside-hydrolyzing beta-glucosidase
LVISKB_0241
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a protopanaxadiol-type ginsenoside with one glucosyl residue at position 3 + H2O = a protopanaxadiol-type ginsenoside with no glycosidic modifications at position 3 + D-glucopyranose
(2)
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a protopanaxadiol-type ginsenoside with two glucosyl residues at position 3 + H2O = a protopanaxadiol-type ginsenoside with one glucosyl residue at position 3 + D-glucopyranose
a protopanaxadiol-type ginsenoside with two glycosyl residues at position 20 + H2O = a protopanaxadiol-type ginsenoside with a single glucosyl residue at position 20 + a monosaccharide
(3)
-
-
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a protopanaxadiol-type ginsenoside with two glucosyl residues at position 3 + H2O = a protopanaxadiol-type ginsenoside with one glucosyl residue at position 3 + D-glucopyranose
(1)
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a protopanaxadiol-type ginsenoside with two glucosyl residues at position 3 + H2O = a protopanaxadiol-type ginsenoside with one glucosyl residue at position 3 + D-glucopyranose
Hydrolysis of the 3-O-beta-D-(1->2)-glucosidic bond, the 3-O-beta-D-glucopyranosyl bond and the 20-O-beta-D-(1->6)-glycosidic bond of protopanaxadiol-type ginsenosides. The enzyme usually leaves a single glucosyl residue attached at position 20 and no glucosyl or one glucosyl residue at position 3. Starting with a ginsenoside that is glycosylated at both positions (e.g. ginsenoside Rb1, Rb2, Rb3, Rc or Rd), the most common products are ginsenoside F2 and ginsenoside C-K with low amounts of ginsenoside Rh2.
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a protopanaxadiol-type ginsenoside with two glucosyl residues at position 3 + H2O = a protopanaxadiol-type ginsenoside with one glucosyl residue at position 3 + D-glucopyranose
Hydrolysis of the 3-O-beta-D-(1->2)-glucosidic bond, the 3-O-beta-D-glucopyranosyl bond and the 20-O-beta-D-(1->6)-glycosidic bond of protopanaxadiol-type ginsenosides. The enzyme usually leaves a single glucosyl residue attached at position 20 and no glucosyl or one glucosyl residue at position 3. Starting with a ginsenoside that is glycosylated at both positions (e.g. ginsenoside Rb1, Rb2, Rb3, Rc or Rd), the most common products are ginsenoside F2 and ginsenoside C-K with low amounts of ginsenoside Rh2.
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ginsenoside glucohydrolase
Ginsenosidase type I is slightly activated by Mg2+ or Ca2+ [1]. The enzyme hydrolyses the 3-O-beta-D-(1->2)-glucosidic bond, the 3-O-beta-D-glucopyranosyl bond and the 20-O-beta-D-(1->6)-glycosidic bond of protopanaxadiol-type ginsenosides. It usually leaves a single glucosyl residue attached at position 20 and one or no glucosyl residues at position 3. Starting with a ginsenoside that is glycosylated at both positions (e.g. ginsenoside Rb1, Rb2, Rb3, Rc or Rd), the most common products are ginsenoside F2 and ginsenoside C-K, with low amounts of ginsenoside Rh2.
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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
ginsenoside Rb1 + H2O
ginsenoside Rh2 + 3 D-glucose
-
via ginsenoside F2
-
-
?
ginsenoside Rb2 + H2O
ginsenoside Rh2 + 2 D-glucose + L-arabinopyranose
-
via ginsenoside F2
-
-
?
ginsenoside Rc + H2O
ginsenoside Rh2 + 2 D-glucose + L-arabinofuranose
-
via ginsenoside F2
-
-
?
ginsenoside Rd + H2O
ginsenoside + D-glucose
-
ginsenoside F2 is a main product plus ginsenoside C-K, produces small amounts of ginsenoside Rh2. Hydrolysis of 3-O-beta-D-(1->2)-glucoside
-
-
?
2-nitrophenyl-beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
93% activity compared to 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
2-nitrophenyl-beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
93% activity compared to 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
4-nitrophenyl-alpha-L-arabinofuranoside + H2O
4-nitrophenol + L-arabinofuranose
-
30% activity compared to 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
4-nitrophenyl-alpha-L-arabinofuranoside + H2O
4-nitrophenol + L-arabinofuranose
Armillaria mellea KACC 50013
-
30% activity compared to 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
4-nitrophenyl-alpha-L-arabinopyranoside + H2O
4-nitrophenol + L-arabinopyranose
-
10% activity compared to 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
4-nitrophenyl-alpha-L-arabinopyranoside + H2O
4-nitrophenol + L-arabinopyranose
Armillaria mellea KACC 50013
-
10% activity compared to 4-nitrophenyl-beta-D-glucopyranoside
-
-
?
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
-
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides Rd and F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
Aspergillus niger g.848
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via ginsenosides Rd and F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
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via ginsenoside F2
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-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenoside F2
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-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenoside F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenoside F2
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-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides F2
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-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides F2
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-
?
ginsenoside Rb1 + H2O
ginsenoside F2 + 2 D-glucose
-
ginsenoside F2 is a main product plus ginsenoside C-K, produces small amounts of ginsenoside Rh2. Hydrolysis of 3-O-beta-D-(1->2)-glucoside and 20-O-beta-D-(1->6)-glucoside
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-
?
ginsenoside Rb1 + H2O
ginsenoside F2 + 2 D-glucose
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ginsenoside F2 is a main product plus ginsenoside C-K, produces small amounts of ginsenoside Rh2. Hydrolysis of 3-O-beta-D-(1->2)-glucoside and 20-O-beta-D-(1->6)-glucoside
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-
?
ginsenoside Rb1 + H2O
ginsenoside F2 + 2 D-glucose
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-
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-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucose
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-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucose
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-
-
-
?
ginsenoside Rb2 + H2O
ginsenoside C-K + 2 D-glucose + L-arabinofuranose
-
-
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?
ginsenoside Rb2 + H2O
ginsenoside C-K + 2 D-glucose + L-arabinofuranose
-
-
-
-
?
ginsenoside Rb2 + H2O
ginsenoside C-K + 2 D-glucose + L-arabinopyranose
-
via ginsenosides Rd and F2
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-
?
ginsenoside Rb2 + H2O
ginsenoside C-K + 2 D-glucose + L-arabinopyranose
Aspergillus niger g.848
-
via ginsenosides Rd and F2
-
-
?
ginsenoside Rb2 + H2O
ginsenoside C-K + 2 D-glucose + L-arabinopyranose
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via ginsenoside F2
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-
?
ginsenoside Rb2 + H2O
ginsenoside C-K + 2 D-glucose + L-arabinopyranose
-
via ginsenoside F2
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-
?
ginsenoside Rb2 + H2O
ginsenoside F2 + D-glucose + L-arabinopyranose
-
-
-
-
?
ginsenoside Rb2 + H2O
ginsenoside F2 + D-glucose + L-arabinopyranose
-
ginsenoside F2 is a main product plus ginsenoside C-K, produces small amounts of ginsenoside Rh2. Hydrolysis of 3-O-beta-D-(1->2)-glucoside and 20-O-alpha-D-(1->6)-arabinopyranoside
-
-
?
ginsenoside Rb2 + H2O
ginsenoside F2 + D-glucose + L-arabinopyranose
-
ginsenoside F2 is a main product plus ginsenoside C-K, produces small amounts of ginsenoside Rh2. Hydrolysis of 3-O-beta-D-(1->2)-glucoside and 20-O-alpha-D-(1->6)-arabinopyranoside
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-
?
ginsenoside Rb2 + H2O
ginsenoside F2 + D-glucose + L-arabinopyranose
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-
-
-
?
ginsenoside Rb2 + H2O
ginsenoside F2 + D-glucose + L-arabinopyranose
-
-
-
-
?
ginsenoside Rb3 + H2O
ginsenoside C-K + 2 D-glucose + xylose
-
via ginsenoside F2
-
-
?
ginsenoside Rb3 + H2O
ginsenoside C-K + 2 D-glucose + xylose
Aspergillus niger g.848
-
via ginsenoside F2
-
-
?
ginsenoside Rb3 + H2O
ginsenoside F2 + D-glucose + D-xylose
-
ginsenoside F2 is a main product plus ginsenoside C-K, produces small amounts of ginsenoside Rh2. Hydrolysis of 3-O-beta-D-(1->2)-glucoside and 20-O-beta-D-(1->6)-xyloside
-
-
?
ginsenoside Rb3 + H2O
ginsenoside F2 + D-glucose + D-xylose
-
ginsenoside F2 is a main product plus ginsenoside C-K, produces small amounts of ginsenoside Rh2. Hydrolysis of 3-O-beta-D-(1->2)-glucoside and 20-O-beta-D-(1->6)-xyloside
-
-
?
ginsenoside Rc + H2O
ginsenoside C-K + 2 D-glucose + L-arabinofuranose
-
via ginsenoside F2
-
-
?
ginsenoside Rc + H2O
ginsenoside C-K + 2 D-glucose + L-arabinofuranose
Aspergillus niger g.848
-
via ginsenoside F2
-
-
?
ginsenoside Rc + H2O
ginsenoside C-K + 2 D-glucose + L-arabinofuranose
-
via ginsenoside F2
-
-
?
ginsenoside Rc + H2O
ginsenoside C-K + 2 D-glucose + L-arabinofuranose
-
via ginsenoside F2
-
-
?
ginsenoside Rc + H2O
ginsenoside F2 + D-glucose + L-arabinofuranose
-
-
-
-
?
ginsenoside Rc + H2O
ginsenoside F2 + D-glucose + L-arabinofuranose
-
ginsenoside F2 is a main product plus ginsenoside C-K, produces small amounts of ginsenoside Rh2. Hydrolysis of 3-O-beta-D-(1->2)-glucoside and 20-O-alpha-D-(1->6)-arabinofuranoside
-
-
?
ginsenoside Rc + H2O
ginsenoside F2 + D-glucose + L-arabinofuranose
-
ginsenoside F2 is a main product plus ginsenoside C-K, produces small amounts of ginsenoside Rh2. Hydrolysis of 3-O-beta-D-(1->2)-glucoside and 20-O-alpha-D-(1->6)-arabinofuranoside
-
-
?
ginsenoside Rc + H2O
ginsenoside F2 + D-glucose + L-arabinofuranose
-
-
-
-
?
ginsenoside Rc + H2O
ginsenoside F2 + D-glucose + L-arabinofuranose
-
-
-
-
?
ginsenoside Rc + H2O
ginsenoside F2 + D-glucose + L-arabinofuranose
-
-
-
-
?
ginsenoside Rd + H2O
ginsenoside F2 + D-glucose
-
-
-
-
?
ginsenoside Rg3 + H2O
ginsenoside Rh2 + D-glucose
-
-
-
-
?
gypenoside XVII + H2O
F2 + D-glucose
-
GypXVI, enzyme mutants W512A and W512K hydrolyze the inner glucose linked to the C-3 position and the outer glucose linked to the C-20 position of GypXVII to produce GypLXXV (cf. EC 3.2.1.191) and F2. Mutant W512R hydrolyzes only the outer glucose linked to the C-20 position of GypXVII to produce F2. The wild-type enzyme hydrolyzes GypXVI only to gypenoside LXXV, GypLXXV
-
-
?
gypenoside XVII + H2O
F2 + D-glucose
-
GypXVI, enzyme mutants W512A and W512K hydrolyze the inner glucose linked to the C-3 position and the outer glucose linked to the C-20 position of GypXVII to produce GypLXXV (cf. EC 3.2.1.191) and F2. Mutant W512R hydrolyzes only the outer glucose linked to the C-20 position of GypXVII to produce F2. The wild-type enzyme hydrolyzes GypXVI only to gypenoside LXXV, GypLXXV
-
-
?
additional information
?
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-
enzyme BG-1 hydrolyzes alpha-(1->6)-arabinofuranosidic linkage at the C-20 site or outer beta-(1->2)-glucosidic linkage at the C-3 site of G-Rc to produce ginsenoside Rd and compound Mc1, respectively. The enzyme also hydrolyzes outer and inner glucosidic linkages at the C-3 site of ginsenoside Rd to produce compound K via ginsenoside F2, and inner glucosidic linkage at the C-3 site of compound Mc1 to produce ginsenoside compound Mc. Compound Mc is also slowly hydrolyzes alpha-(1->6)-arabinofuranosidic linkage at the C-20 site to produce compound K with reaction time prolongation. Finally, the pathways for formation of C-Mc and C-K from G-Rc by enzyme BG-1 are G-Rc -> C-Mc1 -> C-Mc and G-Rc -> G-Rd -> G-F2 -> C-K, respectively. Compound identification by TLC, HPLC, NMR spectroscopic, and UPLC/Q-TOF-MS analysis, detailed overview. No activity with 4-nitrophenyl -alpha-D-glucopyranoside and 4-nitrophenyl-alpha- and -beta-galactopyranoside
-
-
?
additional information
?
-
Armillaria mellea KACC 50013
-
enzyme BG-1 hydrolyzes alpha-(1->6)-arabinofuranosidic linkage at the C-20 site or outer beta-(1->2)-glucosidic linkage at the C-3 site of G-Rc to produce ginsenoside Rd and compound Mc1, respectively. The enzyme also hydrolyzes outer and inner glucosidic linkages at the C-3 site of ginsenoside Rd to produce compound K via ginsenoside F2, and inner glucosidic linkage at the C-3 site of compound Mc1 to produce ginsenoside compound Mc. Compound Mc is also slowly hydrolyzes alpha-(1->6)-arabinofuranosidic linkage at the C-20 site to produce compound K with reaction time prolongation. Finally, the pathways for formation of C-Mc and C-K from G-Rc by enzyme BG-1 are G-Rc -> C-Mc1 -> C-Mc and G-Rc -> G-Rd -> G-F2 -> C-K, respectively. Compound identification by TLC, HPLC, NMR spectroscopic, and UPLC/Q-TOF-MS analysis, detailed overview. No activity with 4-nitrophenyl -alpha-D-glucopyranoside and 4-nitrophenyl-alpha- and -beta-galactopyranoside
-
-
?
additional information
?
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ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
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-
substrates are notoginseng leaf ginsenosides
-
-
?
additional information
?
-
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the enzyme first hydrolyzes the C-20 position 20-O-Glc of ginsenoside Rb1, and then C-3 position 3-O-Glc via a single pathway: Rb1 -> Rd -> F2 -> C-K. It first hydrolyzes 3-O-Glc of ginsenoside Rb2 and Rc, and then 20-O-Ara via a single pathway: Rb2 -> C-O -> C-Y -> C-K and Rc -> C-Mc1 -> C-Mc -> C-K. It mainly hydrolyzes 3-O-Glc of Rb3 via pathway: Rb3 -> C-Mx1 -> C-Mx -> C-K, and slowly hydrolyzes 20-O-Xyl of Rb3 via pathway Rb3 -> Rd -> F2 -> C-K. The average mole yields are 48.2% for compound Mx from ginsenoside Rb3 and compound Mx1, and 41.2% for compound K from other ginsenosides. Products are identified by by TLC and HPLC analysis and NMR spectroscopy. The ability of the pure enzyme to hydrolyze 3-O- and 20-O-glucoside proves that it is a ginsenosidase type-I
-
-
?
additional information
?
-
Aspergillus niger g.848
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
Aspergillus niger g.848
-
substrates are notoginseng leaf ginsenosides
-
-
?
additional information
?
-
Aspergillus niger g.848
-
the enzyme first hydrolyzes the C-20 position 20-O-Glc of ginsenoside Rb1, and then C-3 position 3-O-Glc via a single pathway: Rb1 -> Rd -> F2 -> C-K. It first hydrolyzes 3-O-Glc of ginsenoside Rb2 and Rc, and then 20-O-Ara via a single pathway: Rb2 -> C-O -> C-Y -> C-K and Rc -> C-Mc1 -> C-Mc -> C-K. It mainly hydrolyzes 3-O-Glc of Rb3 via pathway: Rb3 -> C-Mx1 -> C-Mx -> C-K, and slowly hydrolyzes 20-O-Xyl of Rb3 via pathway Rb3 -> Rd -> F2 -> C-K. The average mole yields are 48.2% for compound Mx from ginsenoside Rb3 and compound Mx1, and 41.2% for compound K from other ginsenosides. Products are identified by by TLC and HPLC analysis and NMR spectroscopy. The ability of the pure enzyme to hydrolyze 3-O- and 20-O-glucoside proves that it is a ginsenosidase type-I
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
the enzyme can hydrolyze different glycoside of protopanaxadiol type ginsenosides, can hydrolyze the 3(carbon)-O-beta-glucoside of Rb1, Rb2, Rb3, Rc, Rd, can hydrolyze 20(carbon)-O-beta-glucoside of Rb1, 20-O-beta-xyloside of Rb3, 20-O-alpha-arabinoside(p) of Rb2 and 20-O-alpha-arabinoside(f) of Rc to produce mainly F2, compound-K (C-K) and small Rh2, but can not hydrolyze the glycosides of protopanaxatriol type ginsenoside such as Re, Rf, Rg1
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-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
the enzyme can hydrolyze different glycoside of protopanaxadiol type ginsenosides, can hydrolyze the 3(carbon)-O-beta-glucoside of Rb1, Rb2, Rb3, Rc, Rd, can hydrolyze 20(carbon)-O-beta-glucoside of Rb1, 20-O-beta-xyloside of Rb3, 20-O-alpha-arabinoside(p) of Rb2 and 20-O-alpha-arabinoside(f) of Rc to produce mainly F2, compound-K (C-K) and small Rh2, but can not hydrolyze the glycosides of protopanaxatriol type ginsenoside such as Re, Rf, Rg1
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
recombinant wild-type beta-glucosidase from Clavibacter michiganensis specifically hydrolyzes the outer and inner glucose linked to the C-3 position in protopanaxadiol (PPD)-type ginsenosides (EC 3.2.1.191) and the C-6 position in protopanaxatriol (PPT)-type ginsenosides (EC 3.2.1.194) except for the hydrolysis of gypenoside LXXV (GypLXXV). The enzyme converts gypenoside XVII (GypXVII) to GypLXXV by hydrolyzing the inner glucose linked to the C-3 position
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-
?
additional information
?
-
-
recombinant wild-type beta-glucosidase from Clavibacter michiganensis specifically hydrolyzes the outer and inner glucose linked to the C-3 position in protopanaxadiol (PPD)-type ginsenosides (EC 3.2.1.191) and the C-6 position in protopanaxatriol (PPT)-type ginsenosides (EC 3.2.1.194) except for the hydrolysis of gypenoside LXXV (GypLXXV). The enzyme converts gypenoside XVII (GypXVII) to GypLXXV by hydrolyzing the inner glucose linked to the C-3 position
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
the enzyme from hydrolyzes selectively alpha-(1->6)-arabinofuranosidic linkage at the C-20 position of ginsenoside Rc without attacking any other beta-glucosidic and arabinofuranosidic linkages
-
-
?
additional information
?
-
Ganoderma applanatum KACC 53688
-
the enzyme from hydrolyzes selectively alpha-(1->6)-arabinofuranosidic linkage at the C-20 position of ginsenoside Rc without attacking any other beta-glucosidic and arabinofuranosidic linkages
-
-
?
additional information
?
-
-
the enzyme hydrolyzes selectively alpha-(1->6)-arabinofuranosidic linkage at the C-20 position of ginsenoside Rc without attacking any other beta-glucosidic and arabinofuranosidic linkages
-
-
?
additional information
?
-
Ganoderma lucidum KACC 42231
-
the enzyme hydrolyzes selectively alpha-(1->6)-arabinofuranosidic linkage at the C-20 position of ginsenoside Rc without attacking any other beta-glucosidic and arabinofuranosidic linkages
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
Intrasporangium sp. GS603
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
beta-glucosidase Bgy2 cleaves the outer glucose moieties of ginsenosides at the C-20 position, and the inner glucose at the C-3 position. At optimal conditions, 1.0 mg/ml ginsenoside Rb1 and ginsenoside F2 are converted into 0.59 mg/ml ginsenoside Rd and 0.72mg/ml compound K, with molar conversion productivities of 69% and 91%, respectively. No activity with 4-nitrophenyl-alpha-D-glucopyranoside, 4-nitrophenyl-beta-D-galactopyranoside, 2-nitrophenyl-beta-D-galactopyranoside, and 4-nitrophenyl-alpha-L-arabinofuranoside. Product identification by mass spectrometry
-
-
?
additional information
?
-
beta-glucosidase Bgy2 cleaves the outer glucose moieties of ginsenosides at the C-20 position, and the inner glucose at the C-3 position. At optimal conditions, 1.0 mg/ml ginsenoside Rb1 and ginsenoside F2 are converted into 0.59 mg/ml ginsenoside Rd and 0.72mg/ml compound K, with molar conversion productivities of 69% and 91%, respectively. No activity with 4-nitrophenyl-alpha-D-glucopyranoside, 4-nitrophenyl-beta-D-galactopyranoside, 2-nitrophenyl-beta-D-galactopyranoside, and 4-nitrophenyl-alpha-L-arabinofuranoside. Product identification by mass spectrometry
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
Paecilomyces variotii 229-7
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
bioconversion of major ginsenosides to F2 during milk fermentation
-
-
?
additional information
?
-
-
recombinant His-tagged enzyme BGL hydrolyzes the outer glucose moiety of C-3 and C-20 positions of the major ginsenosides (Rb1 and Rd) and produces the minor ginsenoside F2: the pathway is Rb1 -> Rd -> F2. Furthermore, the enzyme transforms the minor ginsenoside Rg3 to Rh2: pathway Rg3 -> Rh2
-
-
?
additional information
?
-
-
bioconversion of major ginsenosides to F2 during milk fermentation
-
-
?
additional information
?
-
-
recombinant His-tagged enzyme BGL hydrolyzes the outer glucose moiety of C-3 and C-20 positions of the major ginsenosides (Rb1 and Rd) and produces the minor ginsenoside F2: the pathway is Rb1 -> Rd -> F2. Furthermore, the enzyme transforms the minor ginsenoside Rg3 to Rh2: pathway Rg3 -> Rh2
-
-
?
additional information
?
-
-
the enzyme hydrolyzes selectively alpha-(1->6)-arabinofuranosidic linkage at the C-20 position of ginsenoside Rc without attacking any other beta-glucosidic and arabinofuranosidic linkages
-
-
?
additional information
?
-
Pleurotus ostreatus KACC 50356
-
the enzyme hydrolyzes selectively alpha-(1->6)-arabinofuranosidic linkage at the C-20 position of ginsenoside Rc without attacking any other beta-glucosidic and arabinofuranosidic linkages
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
the enzyme hydrolyzes selectively alpha-(1->6)-arabinofuranosidic linkage at the C-20 position of ginsenoside Rc without attacking any other beta-glucosidic and arabinofuranosidic linkages
-
-
?
additional information
?
-
Sanghuangporus baumii KACC 53719
-
the enzyme hydrolyzes selectively alpha-(1->6)-arabinofuranosidic linkage at the C-20 position of ginsenoside Rc without attacking any other beta-glucosidic and arabinofuranosidic linkages
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
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 Rb1 + H2O
ginsenoside Rh2 + 3 D-glucose
-
via ginsenoside F2
-
-
?
ginsenoside Rb2 + H2O
ginsenoside Rh2 + 2 D-glucose + L-arabinopyranose
-
via ginsenoside F2
-
-
?
ginsenoside Rc + H2O
ginsenoside Rh2 + 2 D-glucose + L-arabinofuranose
-
via ginsenoside F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides Rd and F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
Aspergillus niger g.848
-
via ginsenosides Rd and F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenoside F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenoside F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenoside F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenoside F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside C-K + 3 D-glucose
-
via ginsenosides F2
-
-
?
ginsenoside Rb1 + H2O
ginsenoside F2 + 2 D-glucose
-
-
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucose
-
-
-
?
ginsenoside Rb1 + H2O
ginsenoside Rd + D-glucose
-
-
-
-
?
ginsenoside Rb2 + H2O
ginsenoside C-K + 2 D-glucose + L-arabinofuranose
-
-
-
-
?
ginsenoside Rb2 + H2O
ginsenoside C-K + 2 D-glucose + L-arabinofuranose
-
-
-
-
?
ginsenoside Rb2 + H2O
ginsenoside C-K + 2 D-glucose + L-arabinopyranose
-
via ginsenosides Rd and F2
-
-
?
ginsenoside Rb2 + H2O
ginsenoside C-K + 2 D-glucose + L-arabinopyranose
Aspergillus niger g.848
-
via ginsenosides Rd and F2
-
-
?
ginsenoside Rb2 + H2O
ginsenoside C-K + 2 D-glucose + L-arabinopyranose
-
via ginsenoside F2
-
-
?
ginsenoside Rb2 + H2O
ginsenoside C-K + 2 D-glucose + L-arabinopyranose
-
via ginsenoside F2
-
-
?
ginsenoside Rb2 + H2O
ginsenoside F2 + D-glucose + L-arabinopyranose
-
-
-
-
?
ginsenoside Rb2 + H2O
ginsenoside F2 + D-glucose + L-arabinopyranose
-
-
-
-
?
ginsenoside Rb2 + H2O
ginsenoside F2 + D-glucose + L-arabinopyranose
-
-
-
-
?
ginsenoside Rb3 + H2O
ginsenoside C-K + 2 D-glucose + xylose
-
via ginsenoside F2
-
-
?
ginsenoside Rb3 + H2O
ginsenoside C-K + 2 D-glucose + xylose
Aspergillus niger g.848
-
via ginsenoside F2
-
-
?
ginsenoside Rc + H2O
ginsenoside C-K + 2 D-glucose + L-arabinofuranose
-
via ginsenoside F2
-
-
?
ginsenoside Rc + H2O
ginsenoside C-K + 2 D-glucose + L-arabinofuranose
Aspergillus niger g.848
-
via ginsenoside F2
-
-
?
ginsenoside Rc + H2O
ginsenoside C-K + 2 D-glucose + L-arabinofuranose
-
via ginsenoside F2
-
-
?
ginsenoside Rc + H2O
ginsenoside C-K + 2 D-glucose + L-arabinofuranose
-
via ginsenoside F2
-
-
?
ginsenoside Rc + H2O
ginsenoside F2 + D-glucose + L-arabinofuranose
-
-
-
-
?
ginsenoside Rc + H2O
ginsenoside F2 + D-glucose + L-arabinofuranose
-
-
-
-
?
ginsenoside Rc + H2O
ginsenoside F2 + D-glucose + L-arabinofuranose
-
-
-
-
?
ginsenoside Rc + H2O
ginsenoside F2 + D-glucose + L-arabinofuranose
-
-
-
-
?
ginsenoside Rd + H2O
ginsenoside F2 + D-glucose
-
-
-
-
?
ginsenoside Rg3 + H2O
ginsenoside Rh2 + D-glucose
-
-
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
substrates are notoginseng leaf ginsenosides
-
-
?
additional information
?
-
Aspergillus niger g.848
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
Aspergillus niger g.848
-
substrates are notoginseng leaf ginsenosides
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
Intrasporangium sp. GS603
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
Paecilomyces variotii 229-7
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
bioconversion of major ginsenosides to F2 during milk fermentation
-
-
?
additional information
?
-
-
bioconversion of major ginsenosides to F2 during milk fermentation
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
additional information
?
-
-
ginsenosidase type I enzymes simultaneously hydrolyze the sugars linked to C-20 and C-3 in the PPD-type ginsenosides and have broad hydrolysis patterns of A, B, C and D
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Vmax is 79.6 mM/h for Rb1, 45.6 mM/h for Rb2, 1.62 mM/h for Rb3 to Rd, 10.8 mM/h for Rb3 to C-Mx1, and 6.16 mM/h for Rc
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 8.5
activity range, profile overview, recombinant enzyme
4 - 8
-
pH 4.0: about 80% of maximal activity, pH 8.0: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
45 - 50
-
the optimum temperature for compound Mc and compound K formation are slightly different, 55-60°C for C-Mc and 45-50°C for compound K
55 - 60
-
the optimum temperature for compound Mc and compound K formation are slightly different, 55-60°C for C-Mc and 45-50°C for compound K
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 70
20 - 70
-
20°C: about 60% of maximal activity, 70°C: about 60% of maximal activity
20 - 70
about 95% of maximal activity at 20°C, about 30°C at 50°C, and 10% at 70°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Arthrinium sp. GE 17-18
isolated from Panax ginseng roots, an endophytic fungus in Panax ginseng
-
-
brenda
isolated from a fermented food in Korea called kimchi
UniProt
brenda
isolated from a fermented food in Korea called kimchi
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
additional information
evolution
-
the enzyme belongs to the glycosyl hydrolase family 1, GH1
evolution
-
the enzyme belongs to the glycosyl hydrolase family 1, GH1
evolution
-
the enzyme belongs to the glycosyl hydrolase family 1, GH1
evolution
-
Armillaria mellea beta-glucosidase exists in three isomeric forms, BG-1, BG-2 and BG-3, that they exhibit different retention behaviors on DEAE cellulose column and hydrolytic activity toward 4-nitrophenyl beta-D-glucopyranoside. Moreover, when ginsenosides Rc, Rb1 andRd are used as substrates, isozyme BG-1 shows different hydrolytic activity from those of isozymes BG-2 and BG-3
evolution
-
the enzyme belongs to the glycosyl hydrolase family 3, GH3
evolution
the enzyme is a member of glycosyl hydrolase family 3, GH3
evolution
Armillaria mellea KACC 50013
-
Armillaria mellea beta-glucosidase exists in three isomeric forms, BG-1, BG-2 and BG-3, that they exhibit different retention behaviors on DEAE cellulose column and hydrolytic activity toward 4-nitrophenyl beta-D-glucopyranoside. Moreover, when ginsenosides Rc, Rb1 andRd are used as substrates, isozyme BG-1 shows different hydrolytic activity from those of isozymes BG-2 and BG-3
-
evolution
-
the enzyme is a member of glycosyl hydrolase family 3, GH3
-
additional information
-
the amino acid at position 512 in beta-glucosidase from Clavibacter michiganensis determines the regioselectivity for hydrolyzing gypenoside XVII, obtained from the GypXVII-docked homology models of beta-glucosidase. Homology modeling of Clavibacter michiganensis beta-glucosidase based on the crystal structure of beta-D-glucan exohydrolase from Hordeum vulgare (PDB ID 1EX1) as a template
additional information
-
the amino acid at position 512 in beta-glucosidase from Clavibacter michiganensis determines the regioselectivity for hydrolyzing gypenoside XVII, obtained from the GypXVII-docked homology models of beta-glucosidase. Homology modeling of Clavibacter michiganensis beta-glucosidase based on the crystal structure of beta-D-glucan exohydrolase from Hordeum vulgare (PDB ID 1EX1) as a template
-
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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). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
W512A
-
site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows slightly decreased activity with ginsenoside Rb1 and decreased activity with gypenoside XVII compared to the wild-type enzyme. Mutant W512A converts GypXVII to GypLXXV and F2 (cf.. EC 3.2.1.193)
W512K
-
site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows strongly decreased activity with ginsenoside Rb1 and with gypenoside XVII compared to the wild-type enzyme
W512R
-
site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows strongly decreased activity with ginsenoside Rb1 and with gypenoside XVII compared to the wild-type enzyme. mutant W512R containing a positively charged side chain converts GypXVII to F2, cf. EC 3.2.1.193
W512A
-
site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows slightly decreased activity with ginsenoside Rb1 and decreased activity with gypenoside XVII compared to the wild-type enzyme. Mutant W512A converts GypXVII to GypLXXV and F2 (cf.. EC 3.2.1.193)
-
W512K
-
site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows strongly decreased activity with ginsenoside Rb1 and with gypenoside XVII compared to the wild-type enzyme
-
W512R
-
site-directed mutagenesis, mutation of a potential catalytic residue, the mutant shows strongly decreased activity with ginsenoside Rb1 and with gypenoside XVII compared to the wild-type enzyme. mutant W512R containing a positively charged side chain converts GypXVII to F2, cf. EC 3.2.1.193
-
additional information
additional information
-
the hydrolytic pathways of enzyme mutants E83A, R131A, R199A, H238A, E332A, and L509A convert GypXVII to GypLXXV, showing the same regioselectivity as the wild-type enzyme. But mutant W512A converts GypXVII to GypLXXV and F2 (cf. EC 3.2.1.193), indicating that the variant simultaneously hydrolyzes the inner glucose linked to the C-3 position and the outer glucose linked to the C-20 position in GypXVII. Mutant W512F variant enzyme containing an aromatic side chain converts GypXVII as a substrate to GypLXXV, while mutant W512R containing a positively charged side chain converts GypXVII to F2
additional information
-
the hydrolytic pathways of enzyme mutants E83A, R131A, R199A, H238A, E332A, and L509A convert GypXVII to GypLXXV, showing the same regioselectivity as the wild-type enzyme. But mutant W512A converts GypXVII to GypLXXV and F2 (cf. EC 3.2.1.193), indicating that the variant simultaneously hydrolyzes the inner glucose linked to the C-3 position and the outer glucose linked to the C-20 position in GypXVII. Mutant W512F variant enzyme containing an aromatic side chain converts GypXVII as a substrate to GypLXXV, while mutant W512R containing a positively charged side chain converts GypXVII to F2
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 30
purified recombinnat enzyme, pH 7.0, completely stable at
40
purified recombinnat enzyme, pH 7.0, about 85% activity remaining
50
purified recombinnat enzyme, pH 7.0, complete inactivation
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 33.8fold from mycelium by ammonium sulfate fractionation, anion exchange chromatographydialysis, lyophilization, and gel filtration
-
native enzyme from mycelium by anion exchange chromatography to homogeneity
-
recombinant C-terminally His6-tagged enzyme from Lactococcus lactis strain NZ9000 by nickel affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene BglPm, recombinant expression of C-terminally His6-tagged enzyme in Lactococcus lactis strain NZ9000, method optimization
-
gene bgy2, recombinant expression in Escherichia coli strain BL21(DE3)
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain ER2566
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
in pharmaceutical and commercial industries, this recombinant Bgy2 can be suitable for producting ginsenoside Rd and compound K
synthesis
-
production of the pharmacologically active minor ginsenoside F2 from the major ginsenosides Rb1 and Rd by using the recombinant Lactococcus lactis strain expressing heterologous the beta-glucosidase gene
synthesis
-
production of the pharmacologically active minor ginsenoside F2 from the major ginsenosides Rb1 and Rd by using the recombinant Lactococcus lactis strain expressing heterologous the beta-glucosidase gene
-
synthesis
-
in pharmaceutical and commercial industries, this recombinant Bgy2 can be suitable for producting ginsenoside Rd and compound K
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yu, H.; Zhang, C.; Lu, M.; Sun, F.; Fu, Y.; Jin, F.
Purification and characterization of new special ginsenosidase hydrolyzing multi-glycosides of protopanaxadiol ginsenosides, ginsenosidase type I
Chem. Pharm. Bull.
55
231-235
2007
Aspergillus sp., Aspergillus sp. g48p
brenda
Upadhyaya, J.; Yoon, M.S.; Kim, M.J.; Ryu, N.S.; Song, Y.E.; Kim, Y.H.; Kim, M.K.
Purification and characterization of a novel ginsenoside Rc-hydrolyzing beta-glucosidase from Armillaria mellea mycelia
AMB Express
6
112
2016
Armillaria mellea, Ganoderma lucidum, Pleurotus ostreatus, Ganoderma applanatum, Sanghuangporus baumii, Ganoderma lucidum KACC 42231, Armillaria mellea KACC 50013, Pleurotus ostreatus KACC 50356, Ganoderma applanatum KACC 53688, Sanghuangporus baumii KACC 53719
brenda
Shin, K.C.; Hong, S.H.; Seo, M.J.; Oh, D.K.
An amino acid at position 512 in beta-glucosidase from Clavibacter michiganensis determines the regioselectivity for hydrolyzing gypenoside XVII
Appl. Microbiol. Biotechnol.
99
7987-7996
2015
Clavibacter michiganensis, Clavibacter michiganensis DSM 46364
brenda
Shin, K.; Oh, D.
Classification of glycosidases that hydrolyze the specific positions and types of sugar moieties in ginsenosides
Crit. Rev. Biotechnol.
36
1036-1049
2016
Aspergillus niger, Aspergillus oryzae, Aspergillus sp., Microbacterium esteraromaticum, Leuconostoc mesenteroides, Citrus limon, Lactiplantibacillus pentosus, Leuconostoc citreum, Paecilomyces variotii, Sulfolobus acidocaldarius, Saccharolobus solfataricus, Fusobacterium sp., Pseudarthrobacter chlorophenolicus, Intrasporangium sp., Globisporangium irregulare, Nocardioides panaciterrulae, Companilactobacillus paralimentarius, Sphingomonas leidyi, Lactiplantibacillus pentosus 6105, Intrasporangium sp. GS603, Leuconostoc mesenteroides DC102, Leuconostoc citreum LH1, Aspergillus niger g.848, Paecilomyces variotii 229-7
brenda
Li, L.; Shin, S.Y.; Lee, S.J.; Moon, J.S.; Im, W.T.; Han, N.S.
Production of ginsenoside F2 by using Lactococcus lactis with enhanced expression of beta-glucosidase gene from Paenibacillus mucilaginosus
J. Agric. Food Chem.
64
2506-2512
2016
Paenibacillus mucilaginosus, Paenibacillus mucilaginosus KCTC 3870
brenda
Zhong, F.L.; Ma, R.; Jiang, M.; Dong, W.W.; Jiang, J.; Wu, S.; Li, D.; Quan, L.H.
Cloning and characterization of ginsenoside-hydrolyzing beta-glucosidase from Lactobacillus brevis that Ttransforms ginsenosides Rb1 and F2 into ginsenoside Rd and compound K
J. Microbiol. Biotechnol.
26
1661-1667
2016
Levilactobacillus brevis (M5AXT3), Levilactobacillus brevis KB290 (M5AXT3)
brenda
Fu, Y.; Yin, Z.H.; Wu, L.P.; Yin, C.R.
Biotransformation of ginsenoside Rb1 to ginsenoside C-K by endophytic fungus Arthrinium sp. GE 17-18 isolated from Panax ginseng
Lett. Appl. Microbiol.
63
196-201
2016
Arthrinium sp. GE 17-18
brenda
Liu, C.; Zuo, K.; Yu, H.; Sun, C.; Zhang, T.; Xu, L.; Jin, Y.; Im, W.; Jin, F.
Preparation of minor ginsenosides C-Mx and C-K from notoginseng leaf ginsenosides by a special ginsenosidase type-I
Process Biochem.
50
2158-2167
2015
Aspergillus niger, Aspergillus niger g.848
-
brenda
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Release 2023.1 (January 2023)
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