Information on EC 3.2.1.191 - ginsenosidase type III

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Terrabacter ginsenosidimutans

EC NUMBER
COMMENTARY hide
3.2.1.191
-
RECOMMENDED NAME
GeneOntology No.
ginsenosidase type III
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a protopanaxadiol-type ginsenoside with one glucosyl residue at position 3 + H2O = a protopanaxadiol-type ginsenoside with no glycosidic modification at position 3 + D-glucopyranose
show the reaction diagram
(1b)
-
-
-
a protopanaxadiol-type ginsenoside with two glucosyl residues at position 3 + 2 H2O = a protopanaxadiol-type ginsenoside with no glycosidic modification at position 3 + 2 D-glucopyranose
show the reaction diagram
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
show the reaction diagram
(1a)
-
-
-
SYSTEMATIC NAME
IUBMB Comments
protopanaxadiol-type ginsenoside 3-beta-D-hydrolase
Ginsenosidase type III catalyses the sequential hydrolysis of the 3-O-beta-D-(1->2)-glucopyranosyl bond followed by hydrolysis of the 3-O-beta-D-glucopyranosyl bond of protopanaxadiol ginsenosides. When acting for example on ginsenoside Rb1 the enzyme first generates ginsenoside XVII, and subsequently ginsenoside LXXV.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
show the reaction diagram
-
-
-
?
ginsenoside C-Mc1 + H2O
ginsenoside C-Mc + D-glucopyranose
show the reaction diagram
-
hydrolysis of 3-O-beta-D-glucopyranosyl bond
-
-
?
ginsenoside C-Mx1 + H2O
ginsenoside C-Mx + D-glucopyranose
show the reaction diagram
-
hydrolysis of 3-O-beta-D-glucopyranosyl bond
-
-
?
ginsenoside C-O + H2O
ginsenoside C-Y + D-glucopyranose
show the reaction diagram
-
hydrolysis of 3-O-beta-D-glucopyranosyl bond
-
-
?
ginsenoside F2 + H2O
ginsenoside C-K + D-glucopyranose
show the reaction diagram
-
hydrolysis of 3-O-beta-D-glucopyranosyl bond
-
-
?
ginsenoside Rb1 + H2O
gypenoside XVII + D-glucopyranose
show the reaction diagram
ginsenoside Rb2 + H2O
ginsenoside C-O + D-glucopyranose
show the reaction diagram
-
hydrolysis of 3-O-beta-D-(1->2)-glucopyranosyl
-
-
?
ginsenoside Rb3 + H2O
ginsenoside C-Mx1 + D-glucopyranose
show the reaction diagram
-
hydrolysis of 3-O-beta-D-(1->2)-glucopyranosyl bond
-
-
?
ginsenoside Rc + H2O
ginsenoside C-Mc1 + D-glucopyranose
show the reaction diagram
-
hydrolysis of 3-O-beta-D-(1->2)-glucopyranosyl bond
-
-
?
ginsenoside Rd + H2O
ginsenoside F2 + D-glucopyranose
show the reaction diagram
-
hydrolysis of 3-O-beta-D-(1->2)-glucopyranosyl bond
-
-
?
ginsenoside Rg3(S) + H2O
ginsenoside Rh2(S) + D-glucopyranose
show the reaction diagram
-
hydrolysis of 3-O-beta-D-(1->2)-glucopyranosyl bond
-
-
?
ginsenoside Rh2(S) + H2O
protopanaxadiol aglycone + D-glucopyranose
show the reaction diagram
-
hydrolysis of 3-O-beta-D-glucopyranosyl bond
-
-
?
gypenoside XVII + H2O
gypenoside LXXV + D-glucopyranose
show the reaction diagram
additional information
?
-
-
the enzyme is able to hydrolyse 3-O-glucoside of multi-protopanaxadiol-type ginsenosides. Similarly, the enzyme can hydrolyse the glucopyranosyls linked to the 3-O-position of Rb2, Rc, Rd, Rb3, and Rg3
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the enzyme does not require Mg2+, Mn2+, Co2+, Zn2+, Ca2+, or Cu2+ for activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Hg2+
-
10 mM, complete inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.2
4-nitrophenyl beta-D-glucopyranoside
-
pH 7.0, 37C
12.9
ginsenoside F2
-
pH 7.0, 40C
0.14 - 4.08
ginsenoside Rb1
9.09
ginsenoside Rb2
-
pH 7.0, 40C
8.85
ginsenoside Rb3
-
pH 7.0, 40C
3.85
ginsenoside Rc
-
pH 7.0, 40C
11.4
ginsenoside Rd
-
pH 7.0, 40C
9.7
ginsenoside Rg3(S)
-
pH 7.0, 40C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
the enzyme retains over 82% of its optimal activity between pH values 6.0 and 8.0. It exhibits residual activity at pH 5.0, 9.0, and 10.0, and it shows no activity at pH 4.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
-
3 * 70000, SDS-PAGE
72000
-
x * 72000, SDS-PAGE
193000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 71140, calculated from sequence; x * 72000, SDS-PAGE
trimer
-
3 * 70000, SDS-PAGE; 3 * 71140, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
the enzyme is stable at temperatures lower than 37C
45
-
about 32% of the activity is lost after incubation at 45C for 30 min
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli