BRENDA - Enzyme Database show
show all sequences of 3.2.1.195

A new ginsenosidase from Aspergillus strain hydrolyzing 20-O-multi-glycoside of PPD ginsenoside

Yu, H.; Liu, Q.; Zhang, C.; Lu, M.; Fu, Y.; Im, W.-T.; Jin, F.; Proc. Biochem. 44, 772-775 (2009)
No PubMed abstract available

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
Cu2+
-
Aspergillus sp.
Pb2+
-
Aspergillus sp.
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
50100 mM slightly enhances the ginsenosidase type II activity
Aspergillus sp.
Mg2+
50100 mM slightly enhances the ginsenosidase type II activity
Aspergillus sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
60000
-
x * 60000, SDS-PAGE
Aspergillus sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aspergillus sp.
-
-
-
Aspergillus sp. g48p
-
-
-
Purification (Commentary)
Commentary
Organism
-
Aspergillus sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ginsenoside Rb1 + H2O
the enzyme hydrolyzes the 20-O-beta-D-(1->6)-glucoside
723612
Aspergillus sp.
ginsenoside Rd + D-glucose
the enzyme produces mainly ginsenoside Rd, and small amount of ginsenoside 20(S)-Rg3
-
-
?
ginsenoside Rb1 + H2O
the enzyme hydrolyzes the 20-O-beta-D-(1->6)-glucoside
723612
Aspergillus sp. g48p
ginsenoside Rd + D-glucose
the enzyme produces mainly ginsenoside Rd, and small amount of ginsenoside 20(S)-Rg3
-
-
?
ginsenoside Rb2 + H2O
the enzyme hydrolyzes the 20-O-alpha-(1->6)-arabinopyranoside
723612
Aspergillus sp.
ginsenoside Rd + L-arabinopyranose
the enzyme produces mainly ginsenoside Rd, and small amount of ginsenoside 20(S)-Rg3
-
-
?
ginsenoside Rb2 + H2O
the enzyme hydrolyzes the 20-O-alpha-(1->6)-arabinopyranoside
723612
Aspergillus sp. g48p
ginsenoside Rd + L-arabinopyranose
the enzyme produces mainly ginsenoside Rd, and small amount of ginsenoside 20(S)-Rg3
-
-
?
ginsenoside Rb3 + H2O
the enzyme hydrolyzes the 20-O-beta-(1->6)-xyloside
723612
Aspergillus sp.
ginsenoside Rd + D-xylose
the enzyme produces mainly ginsenoside Rd, and small amount of ginsenoside 20(S)-Rg3
-
-
?
ginsenoside Rb3 + H2O
the enzyme hydrolyzes the 20-O-beta-(1->6)-xyloside
723612
Aspergillus sp. g48p
ginsenoside Rd + D-xylose
the enzyme produces mainly ginsenoside Rd, and small amount of ginsenoside 20(S)-Rg3
-
-
?
ginsenoside Rc + H2O
the enzyme hydrolyzes the 20-O-alpha-(1->6)-arabinofuranoside
723612
Aspergillus sp.
ginsenoside Rd + L-arabinofuranose
the enzyme produces mainly ginsenoside Rd, and small amount of ginsenoside 20(S)-Rg3
-
-
?
ginsenoside Rc + H2O
the enzyme hydrolyzes the 20-O-alpha-(1->6)-arabinofuranoside
723612
Aspergillus sp. g48p
ginsenoside Rd + L-arabinofuranose
the enzyme produces mainly ginsenoside Rd, and small amount of ginsenoside 20(S)-Rg3
-
-
?
ginsenoside Rd + H2O
slowly hydrolyzes the 20-O-glucoside of Rd to produce very small amounts of ginsenoside Rg3
723612
Aspergillus sp.
ginsenoside Rg3 + D-glucose
-
-
-
?
additional information
ginsenosidase type II does not hydrolyze the 3-O-beta-glucoside of Rb1, Rb2, Rb3. Ginsenosidase type II does not hydrolyze the glycosides of protopanaxatriol type ginsenoside such as Re, Rf, Rg1
723612
Aspergillus sp.
?
-
-
-
-
additional information
ginsenosidase type II does not hydrolyze the 3-O-beta-glucoside of Rb1, Rb2, Rb3. Ginsenosidase type II does not hydrolyze the glycosides of protopanaxatriol type ginsenoside such as Re, Rf, Rg1
723612
Aspergillus sp. g48p
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 60000, SDS-PAGE
Aspergillus sp.
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
40
-
assay at
Aspergillus sp.
50
-
-
Aspergillus sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
-
-
Aspergillus sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cu2+
-
Aspergillus sp.
Pb2+
-
Aspergillus sp.
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
50100 mM slightly enhances the ginsenosidase type II activity
Aspergillus sp.
Mg2+
50100 mM slightly enhances the ginsenosidase type II activity
Aspergillus sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
60000
-
x * 60000, SDS-PAGE
Aspergillus sp.
Purification (Commentary) (protein specific)
Commentary
Organism
-
Aspergillus sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ginsenoside Rb1 + H2O
the enzyme hydrolyzes the 20-O-beta-D-(1->6)-glucoside
723612
Aspergillus sp.
ginsenoside Rd + D-glucose
the enzyme produces mainly ginsenoside Rd, and small amount of ginsenoside 20(S)-Rg3
-
-
?
ginsenoside Rb1 + H2O
the enzyme hydrolyzes the 20-O-beta-D-(1->6)-glucoside
723612
Aspergillus sp. g48p
ginsenoside Rd + D-glucose
the enzyme produces mainly ginsenoside Rd, and small amount of ginsenoside 20(S)-Rg3
-
-
?
ginsenoside Rb2 + H2O
the enzyme hydrolyzes the 20-O-alpha-(1->6)-arabinopyranoside
723612
Aspergillus sp.
ginsenoside Rd + L-arabinopyranose
the enzyme produces mainly ginsenoside Rd, and small amount of ginsenoside 20(S)-Rg3
-
-
?
ginsenoside Rb2 + H2O
the enzyme hydrolyzes the 20-O-alpha-(1->6)-arabinopyranoside
723612
Aspergillus sp. g48p
ginsenoside Rd + L-arabinopyranose
the enzyme produces mainly ginsenoside Rd, and small amount of ginsenoside 20(S)-Rg3
-
-
?
ginsenoside Rb3 + H2O
the enzyme hydrolyzes the 20-O-beta-(1->6)-xyloside
723612
Aspergillus sp.
ginsenoside Rd + D-xylose
the enzyme produces mainly ginsenoside Rd, and small amount of ginsenoside 20(S)-Rg3
-
-
?
ginsenoside Rb3 + H2O
the enzyme hydrolyzes the 20-O-beta-(1->6)-xyloside
723612
Aspergillus sp. g48p
ginsenoside Rd + D-xylose
the enzyme produces mainly ginsenoside Rd, and small amount of ginsenoside 20(S)-Rg3
-
-
?
ginsenoside Rc + H2O
the enzyme hydrolyzes the 20-O-alpha-(1->6)-arabinofuranoside
723612
Aspergillus sp.
ginsenoside Rd + L-arabinofuranose
the enzyme produces mainly ginsenoside Rd, and small amount of ginsenoside 20(S)-Rg3
-
-
?
ginsenoside Rc + H2O
the enzyme hydrolyzes the 20-O-alpha-(1->6)-arabinofuranoside
723612
Aspergillus sp. g48p
ginsenoside Rd + L-arabinofuranose
the enzyme produces mainly ginsenoside Rd, and small amount of ginsenoside 20(S)-Rg3
-
-
?
ginsenoside Rd + H2O
slowly hydrolyzes the 20-O-glucoside of Rd to produce very small amounts of ginsenoside Rg3
723612
Aspergillus sp.
ginsenoside Rg3 + D-glucose
-
-
-
?
additional information
ginsenosidase type II does not hydrolyze the 3-O-beta-glucoside of Rb1, Rb2, Rb3. Ginsenosidase type II does not hydrolyze the glycosides of protopanaxatriol type ginsenoside such as Re, Rf, Rg1
723612
Aspergillus sp.
?
-
-
-
-
additional information
ginsenosidase type II does not hydrolyze the 3-O-beta-glucoside of Rb1, Rb2, Rb3. Ginsenosidase type II does not hydrolyze the glycosides of protopanaxatriol type ginsenoside such as Re, Rf, Rg1
723612
Aspergillus sp. g48p
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 60000, SDS-PAGE
Aspergillus sp.
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
40
-
assay at
Aspergillus sp.
50
-
-
Aspergillus sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5
-
-
Aspergillus sp.
Other publictions for EC 3.2.1.195
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
738475
Xie
Characterization of a novel ar ...
Pseudothermotoga thermarum, Pseudothermotoga thermarum DSM 5069
J. Appl. Microbiol.
120
647-660
2016
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1
1
-
-
-
2
-
-
-
1
-
3
2
-
-
-
-
-
-
-
-
2
1
1
1
-
-
1
-
1
-
-
-
-
-
1
1
-
-
-
-
-
2
-
-
-
-
1
-
3
-
-
-
-
-
-
-
2
1
1
1
-
-
1
-
1
-
-
-
-
-
-
-
723612
Yu
-
A new ginsenosidase from Asper ...
Aspergillus sp., Aspergillus sp. g48p
Proc. Biochem.
44
772-775
2009
-
-
-
-
-
-
2
-
-
2
1
-
-
3
-
-
1
-
-
-
-
-
11
1
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
2
1
-
-
-
-
1
-
-
-
-
11
1
2
-
-
-
1
-
-
-
-
-
-
-
-
-