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Information on EC 3.2.1.186 - protodioscin 26-O-beta-D-glucosidase
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EC Tree
3.2.1.186 protodioscin 26-O-beta-D-glucosidaseIUBMB Comments
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.
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Word Map
- 3.2.1.186
-
german
- beta-glucosidase
- torvum
- ceramide
-
questionnaire-9
- solanum
-
desaturase
- dihydroceramide
The enzyme appears in viruses and cellular organisms
Synonyms
sbgl3, torvosidase, csf26g1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
torvosidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protodioscin + H2O = 26-deglucoprotodioscin + D-glucose
-
-
-
-
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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.
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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
avenacoside + H2O
26-deglucoavenacoside + D-glucose
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
-
-
?
dalcochinin 8'-beta-D-glucoside + H2O
?
-
the natural substrate of Thai rosewood beta-glucosidase. 24% of the activity with torvoside A
-
-
?
decyl-beta-D-glucoside + H2O
decanol + D-glucose
83% activity compared to torvoside A
-
-
?
hexyl-beta-D-glucoside + H2O
hexanol + D-glucose
43% activity compared to torvoside A
-
-
?
octyl-beta-D-glucoside + H2O
octanol + D-glucose
69% activity compared to torvoside A
-
-
?
phenyl-beta-D-glucoside + H2O
phenol + D-glucose
36% activity compared to torvoside A
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferol + D-glucopyranose
-
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferol + D-glucopyranose
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
?
avenacoside A + H2O
26-deglucoavenacoside A + D-glucose
the enzyme belongs to a preformed defence system of oat against fungal infection
-
-
?
avenacoside A + H2O
26-deglucoavenacoside A + D-glucose
-
the enzyme in plastid hydrolyzes avenacosides to C26-degluco-avenacosides to combat against fungal infections
-
-
?
avenacoside B + H2O
26-deglucoavenacoside B + D-glucose
the enzyme belongs to a preformed defence system of oat against fungal infection
-
-
?
avenacoside B + H2O
26-deglucoavenacoside B + D-glucose
-
the enzyme in plastid hydrolyzes avenacosides to C26-degluco-avenacosides to combat against fungal infections
-
-
?
protodioscin + H2O
26-deglucoprotodioscin + D-glucose
-
-
-
?
protogracillin
26-deglucoprotogracillin + D-glucose
the enzyme is highly specific for cleavage of the C26-bound glucose moiety of furostanol glycosides
-
-
?
torvoside A + H2O
26-deglucotorvoside A + D-glucose
best substrate for native and recombinant enzymes
-
-
?
additional information
?
-
4-nitrophenyl derivatives serve as substrates, in decreasing order: beta-fucoside, beta-glucoside, beta-galactoside, beta-xyloside. The corresponding 2-nitrophenyl glycosides are less well accepted. No hydrolysis is found with alpha-glycosides and beta-thioglucoside
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
no activity amygdalin, cellobiose, gentiobiose, octyl beta-D-glucoside or prunasin
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl beta-D-fucoside, 4-nitrophenyl beta-L-fucoside, 4-nitrophenyl beta-D-xyloside, 4-nitrophenyl beta-D-galactoside, 4-nitrophenyl beta-D-N-acetylglucosaminide, 4-nitrophenyl beta-D-mannoside, amygdalin, laminarin, prunasin, glucosinolate (sinigrin), aromatic glucosides (arbutin, salicin), indoxyl-beta-D-glucoside, methyl-beta-D-glucoside, cellobiose, cellotriose, cellotetraose, laminaribiose, laminaritriose, laminaritetraose and gentiobiose
-
-
?
additional information
?
-
the beta-glucosidase (torvosidase) purified from Solanum torvum leaves specifically catalyzes the hydrolysis of two furostanol 26-O-beta-glucosides, torvosides A and H
-
-
?
additional information
?
-
-
the beta-glucosidase (torvosidase) purified from Solanum torvum leaves specifically catalyzes the hydrolysis of two furostanol 26-O-beta-glucosides, torvosides A and H
-
-
?
additional information
?
-
the beta-glucosidase (torvosidase) purified from Solanum torvum leaves specifically catalyzes the hydrolysis of two furostanol 26-O-beta-glucosides, torvosides A and H. No activity with (1,2)-beta-linked glucobiose and (1,3)-beta-linked glucobiose, and with beta-linked oligosaccharides, namely cellobiose, cellotriose, cellotetraose, laminaribiose, laminaritriose, laminaritetraose, and gentiobiose
-
-
?
additional information
?
-
-
the beta-glucosidase (torvosidase) purified from Solanum torvum leaves specifically catalyzes the hydrolysis of two furostanol 26-O-beta-glucosides, torvosides A and H. No activity with (1,2)-beta-linked glucobiose and (1,3)-beta-linked glucobiose, and with beta-linked oligosaccharides, namely cellobiose, cellotriose, cellotetraose, laminaribiose, laminaritriose, laminaritetraose, and gentiobiose
-
-
?
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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
avenacoside + H2O
26-deglucoavenacoside + D-glucose
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
the enzyme belongs to a preformed defence system of oat against fungal infection
-
-
?
avenacoside A + H2O
26-deglucoavenacoside A + D-glucose
-
the enzyme in plastid hydrolyzes avenacosides to C26-degluco-avenacosides to combat against fungal infections
-
-
?
avenacoside B + H2O
26-deglucoavenacoside B + D-glucose
the enzyme belongs to a preformed defence system of oat against fungal infection
-
-
?
avenacoside B + H2O
26-deglucoavenacoside B + D-glucose
-
the enzyme in plastid hydrolyzes avenacosides to C26-degluco-avenacosides to combat against fungal infections
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
the beta-glucosidase (torvosidase) purified from Solanum torvum leaves specifically catalyzes the hydrolysis of two furostanol 26-O-beta-glucosides, torvosides A and H
-
-
?
additional information
?
-
-
the beta-glucosidase (torvosidase) purified from Solanum torvum leaves specifically catalyzes the hydrolysis of two furostanol 26-O-beta-glucosides, torvosides A and H
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.66
4-methylumbelliferyl beta-D-glucoside
recombinant His-tagged enzyme, pH 5.0, 37°C
1.01
4-nitrophenyl beta-D-glucoside
recombinant His-tagged enzyme, pH 5.0, 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.7
4-methylumbelliferyl beta-D-glucoside
recombinant His-tagged enzyme, pH 5.0, 37°C
4.9
4-nitrophenyl beta-D-glucoside
recombinant His-tagged enzyme, pH 5.0, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.12
4-methylumbelliferyl beta-D-glucoside
recombinant His-tagged enzyme, pH 5.0, 37°C
10.6
4-methylumbelliferyl beta-D-glucoside
recombinant His-tagged enzyme, pH 5.0, 37°C
4.85
4-nitrophenyl beta-D-glucoside
recombinant His-tagged enzyme, pH 5.0, 37°C
8.8
4-nitrophenyl beta-D-glucoside
recombinant His-tagged enzyme, pH 5.0, 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
purified recombinant His-tagged enzyme, substrate torvoside A, pH 5.0, 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
quantitative real-time PCR expression analysis
brenda
additional information
-
quantitative real-time PCR expression analysis
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
torvosidase is classified as a glycosyl hydrolase family GH3 beta-glucosidase, but cannot hydrolyze beta-oligoglucosides, the natural substratesof GH3 enzymes. Its substrates, furostanol glycoside 26-O-beta-glucosides, are reported as natural substrates of some plant GH1 enzymes
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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). F26G_HELSP
562
0
63649
Swiss-Prot
Chloroplast (Reliability: 3)
F26G_SOLTO
61
0
6766
Swiss-Prot
other Location (Reliability: 4)
A0A2P6QM48_ROSCH
56
0
6572
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2G9GE32_9LAMI
656
1
72413
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2G9H7L4_9LAMI
636
1
69356
TrEMBL
Secretory Pathway (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
x * 60000, the enzyme is highly aggregated. It consists of 300-350 kDa aggregates and multimers thereof
87000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
multimer
x * 60000, the enzyme is highly aggregated. It consists of 300-350 kDa aggregates and multimers thereof
additional information
-
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
monomer
1 * 66573, sequence calculation, 1 * 80700, native enzyme, SDS-PAGE, 1 * 140000, glycosylated recombinant His-tagged enzyme, SDS-PAGE, 1 * 70000, deglycosylated recombinant His-tagged enzyme, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
the native enzyme is glycosylated, while the recombinant enzyme is hyperglycosylated, deglycosylation by endoglycosidase H (EndoH) shifting the molecular weight from 140 to 70 kDa
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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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme 323fold from Pichia pastoris by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene bgl3, DNA and amino acid sequence determiantion and analysis, sequence comparisons, quantitative real-time PCR expression analysis, recombinant expression of His-tagged enzyme in Pichia pastoris with post-translational glycosylation
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, S.Y.; Kim, Y.W.; Hegerl, R.; Cyrklaff, M.; Kim, I.S.
Novel type of enzyme multimerization enhances substrate affinity of oat beta-glucosidase
J. Struct. Biol.
150
1-10
2005
Avena sativa
brenda
Gus-Mayer, S.; Brunner, H.; Schneider-Poetsch, H.A.; Lottspeich, F.; Eckerskorn, C.; Grimm, R.; Rdiger, W.
The amino acid sequence previously attributed to a protein kinase or a TCP1-related molecular chaperone and co-purified with phytochrome is a beta-glucosidase
FEBS Lett.
347
51-54
1994
Avena sativa (Q38786)
brenda
Inoue, K.; Ebizuka, Y.
Purification and characterization of furostanol glycoside 26-O-beta-glucosidase from Costus speciosus rhizomes
FEBS Lett.
378
157-160
1996
Hellenia speciosa (Q42707)
brenda
Inoue, K.; Shibuya, M.; Yamamoto, K.; Ebizuka, Y.
Molecular cloning and bacterial expression of a cDNA encoding furostanol glycoside 26-O-beta-glucosidase of Costus speciosus
FEBS Lett.
389
273-277
1996
Hellenia speciosa (Q42707), Hellenia speciosa
brenda
Arthan, D.; Kittakoop, P.; Esen, A.; Svasti, J.
Furostanol glycoside 26-O-beta-glucosidase from the leaves of Solanum torvum
Phytochemistry
67
27-33
2006
Solanum torvum
brenda
Gus-Mayer, S.; Brunner, H.; Schneider-Poetsch, H.A.
Rdiger, W.: Avenacosidase from oat: purification, sequence analysis and biochemical characterization of a new member of the BGA family of beta-glucosidases
Plant Mol. Biol.
26
909-921
1994
Avena sativa (Q38786)
brenda
Suthangkornkul, R.; Sriworanun, P.; Nakai, H.; Okuyama, M.; Svasti, J.; Kimura, A.; Senapin, S.; Arthan, D.
A Solanum torvum GH3 beta-glucosidase expressed in Pichia pastoris catalyzes the hydrolysis of furostanol glycoside
Phytochemistry
127
4-11
2016
Solanum torvum (P0DKH4), Solanum torvum
brenda
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