Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.2.1.186 - protodioscin 26-O-beta-D-glucosidase and Organism(s) Avena sativa and UniProt Accession Q38786

for references in articles please use BRENDA:EC3.2.1.186
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB 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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Avena sativa
UNIPROT: Q38786
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Avena sativa
The enzyme appears in selected viruses and cellular organisms
Synonyms
sbgl3, torvosidase, csf26g1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
avenacosidase
-
aveconasidase
-
-
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-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
-
-
?
avenacoside A + H2O
26-deglucoavenacoside A + D-glucose
show the reaction diagram
avenacoside B + H2O
26-deglucoavenacoside B + D-glucose
show the reaction diagram
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
?
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
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
the enzyme belongs to a preformed defence system of oat against fungal infection
-
-
?
avenacoside B + H2O
26-deglucoavenacoside B + D-glucose
show the reaction diagram
the enzyme belongs to a preformed defence system of oat against fungal infection
-
-
?
avenacoside A + H2O
26-deglucoavenacoside A + D-glucose
show the reaction diagram
-
the enzyme in plastid hydrolyzes avenacosides to C26-degluco-avenacosides to combat against fungal infections
-
-
?
avenacoside B + H2O
26-deglucoavenacoside B + D-glucose
show the reaction diagram
-
the enzyme in plastid hydrolyzes avenacosides to C26-degluco-avenacosides to combat against fungal infections
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AVCO1_AVESA
574
0
65041
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
x * 60000, the enzyme is highly aggregated. It consists of 300-350 kDa aggregates and multimers thereof
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team