Information on EC 3.2.1.186 - protodioscin 26-O-beta-D-glucosidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.2.1.186
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RECOMMENDED NAME
GeneOntology No.
protodioscin 26-O-beta-D-glucosidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
protodioscin + H2O = 26-deglucoprotodioscin + D-glucose
show the reaction diagram
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-
-
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SYSTEMATIC NAME
IUBMB Comments
protodioscin glucohydrolase
The enzyme has been characterized from the plants Cheilocostus speciosus and Solanum torvum. It also hydrolyses the 26-beta-D-glucose group from related steroid glucosides such as protogracillin, torvoside A and torvoside H.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferol + D-glucopyranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
show the reaction diagram
-
-
-
-
?
avenacoside + H2O
26-deglucoavenacoside + D-glucose
show the reaction diagram
the enzyme is part of the defense system of Arena sativa. Avenacosides are hydrolyzed to 26-desgluco-avenacosides immediately after damage of the plant tissue. Only the desgluco-derivatives exhibit fungicidal activity
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-
?
avenacoside A + H2O
26-deglucoavenacoside A + D-glucose
show the reaction diagram
avenacoside B + H2O
26-deglucoavenacoside B + D-glucose
show the reaction diagram
dalcochinin 8'-beta-D-glucoside + H2O
?
show the reaction diagram
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the natural substrate of Thai rosewood beta-glucosidase. 24% of the activity with torvoside A
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-
?
protodioscin + H2O
26-deglucoprotodioscin + D-glucose
show the reaction diagram
protogracillin + H2O
26-deglucoprotogracillin + D-glucose
show the reaction diagram
torvoside A + H2O
26-deglucotorvoside A + D-glucose
show the reaction diagram
-
-
-
-
?
torvoside H + H2O
26-deglucotorvoside H + D-glucose
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
avenacoside + H2O
26-deglucoavenacoside + D-glucose
show the reaction diagram
Q38786
the enzyme is part of the defense system of Arena sativa. Avenacosides are hydrolyzed to 26-desgluco-avenacosides immediately after damage of the plant tissue. Only the desgluco-derivatives exhibit fungicidal activity
-
-
?
avenacoside A + H2O
26-deglucoavenacoside A + D-glucose
show the reaction diagram
avenacoside B + H2O
26-deglucoavenacoside B + D-glucose
show the reaction diagram
additional information
?
-
Q42707
the enzyme is involved in the postharvest conversion of furostanol glycosides to spirostanol glycosides in Costus speciosus. Furostanol glycosides are the precursors of spirostane glycosides, containing a glucose unit attached to the C-26 hydroxyl of the aglycone
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-sitosterol
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cholesterol
-
-
conduritol beta-epoxide
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-
D-glucono-1,5-lactone
diosgenin
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0.079, 50% inhibition
Hg2+
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1 mM, 88% loss of activity
Mg2+
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1 mM, 10% inhibition
Zn2+
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1 mM, 12% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.78
4-methylumbelliferyl beta-D-glucoside
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pH 5.0, 37°C
1.03
4-nitrophenyl beta-D-glucoside
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pH 5.0, 37°C
0.05
protogracillin
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pH 5.0, 40°C
0.063
torvoside A
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pH 5.0, 37°C
0.068
torvoside H
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pH 5.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.3
4-methylumbelliferyl beta-D-glucoside
Solanum torvum
-
pH 5.0, 37°C
9.1
4-nitrophenyl beta-D-glucoside
Solanum torvum
-
pH 5.0, 37°C
8.6
torvoside A
Solanum torvum
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pH 5.0, 37°C
7.7
torvoside H
Solanum torvum
-
pH 5.0, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10.7
4-methylumbelliferyl beta-D-glucoside
Solanum torvum
-
pH 5.0, 37°C
1709
8.8
4-nitrophenyl beta-D-glucoside
Solanum torvum
-
pH 5.0, 37°C
712
136.5
torvoside A
Solanum torvum
-
pH 5.0, 37°C
42476
113
torvoside H
Solanum torvum
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pH 5.0, 37°C
42477
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4
beta-sitosterol
Cheilocostus speciosus
-
pH 5.0, 40°C
2.8
cholesterol
Cheilocostus speciosus
-
pH 5.0, 40°C
2.4
conduritol beta-epoxide
Cheilocostus speciosus
-
pH 5.0, 40°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
325
-
pH 5.0, 40°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 5.5
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substrate: protogracillin
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.8
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
-
1 * 54000 + 1 * 58000, SDS-PAGE
58000
-
1 * 54000 + 1 * 58000, SDS-PAGE
60000
-
x * 60000, the enzyme is highly aggregated. It consists of 300-350 kDa aggregates and multimers thereof
80700
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1 * 80700, SDS-PAGE
87000
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gel filtration
110000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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1 * 54000 + 1 * 58000, SDS-PAGE
monomer
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1 * 80700, SDS-PAGE
multimer
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x * 60000, the enzyme is highly aggregated. It consists of 300-350 kDa aggregates and multimers thereof
additional information
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the enzyme has a quaternary protein structure of a three-dimensionally radiated assembly of long fibrillae. It is assembled by linear stacking of hollow trimeric units and the resulting fibril has a long central tunnel connecting to the outer medium via regularly distributed side fenestrations. The enzyme active sites are located within the central tunnel. This unique multimer assembly increases enzyme affinity to avenacosides, in vivo substrates, and may function to discriminate avenacosides from many other kinds of beta-glucoside in oat. The fibrillar multimer of oat beta-glucosidase is a novel quaternary protein structure for enzyme supramolecular assembly that may have a functional role in the regulation of enzyme affinity
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is highly aggregated. It consists of 300-350 kDa aggregates and multimers thereof. Dissociation by freezing and thawing leads to complete loss of enzyme activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 20 mM potassium phosphate buffer, pH 7.0, stable for 3 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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