Novel type of enzyme multimerization enhances substrate affinity of oat beta-glucosidase
Kim, S.Y.; Kim, Y.W.; Hegerl, R.; Cyrklaff, M.; Kim, I.S.; J. Struct. Biol. 150, 1-10 (2005) 
Data extracted from this reference:
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
3.2.1.21
glucono(1-5)lactone
-
Avena sativa
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.2.1.21
additional information
-
additional information
kinetics of multimers of different size, overview, effects of active site modifcation by N-(dimethylaminopropyl)-N'-ethylcarbodiimide hydrochloride on kinetics, overview
Avena sativa
3.2.1.21
0.063
-
avenacoside
pH 6.8, 30°C, hexameric enzyme form
Avena sativa
3.2.1.21
2.3
-
4-nitrophenyl beta-D-glucopyranoside
pH 6.8, 30°C, hexameric enzyme form
Avena sativa
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.2.1.21
plastid
-
Avena sativa
9536
-
3.2.1.186
plastid
-
Avena sativa
9536
-
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
3.2.1.21
avenacoside + H2O
Avena sativa
the enzyme hydrolyzes the avenacosides to combat fungal attack
C26-desgluco-avenacosides + beta-D-glucose
-
-
?
3.2.1.21
genistin + H2O
Avena sativa
-
?
-
-
?
3.2.1.186
avenacoside A + H2O
Avena sativa
the enzyme in plastid hydrolyzes avenacosides to C26-degluco-avenacosides to combat against fungal infections
26-deglucoavenacoside A + D-glucose
-
-
?
3.2.1.186
avenacoside B + H2O
Avena sativa
the enzyme in plastid hydrolyzes avenacosides to C26-degluco-avenacosides to combat against fungal infections
26-deglucoavenacoside B + D-glucose
-
-
?
Organism
EC Number
Organism
UniProt
Commentary
Textmining
3.2.1.21
Avena sativa
-
type I enzyme
-
3.2.1.186
Avena sativa
-
-
-
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
3.2.1.21
seedling
etiolated
Avena sativa
-
3.2.1.186
leaf
-
Avena sativa
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
3.2.1.21
4-nitrophenyl beta-D-glucopyranoside + H2O
-
666175
Avena sativa
4-nitrophenol + beta-D-glucose
-
-
-
?
3.2.1.21
avenacoside + H2O
-
666175
Avena sativa
C26-desgluco-avenacosides + beta-D-glucose
-
-
-
?
3.2.1.21
avenacoside + H2O
the enzyme hydrolyzes the avenacosides to combat fungal attack
666175
Avena sativa
C26-desgluco-avenacosides + beta-D-glucose
-
-
-
?
3.2.1.21
genistin + H2O
-
666175
Avena sativa
?
-
-
-
?
3.2.1.186
avenacoside A + H2O
-
666175
Avena sativa
26-deglucoavenacoside A + D-glucose
-
-
-
?
3.2.1.186
avenacoside A + H2O
the enzyme in plastid hydrolyzes avenacosides to C26-degluco-avenacosides to combat against fungal infections
666175
Avena sativa
26-deglucoavenacoside A + D-glucose
-
-
-
?
3.2.1.186
avenacoside B + H2O
-
666175
Avena sativa
26-deglucoavenacoside B + D-glucose
-
-
-
?
3.2.1.186
avenacoside B + H2O
the enzyme in plastid hydrolyzes avenacosides to C26-degluco-avenacosides to combat against fungal infections
666175
Avena sativa
26-deglucoavenacoside B + D-glucose
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
3.2.1.21
More
quarternary structure analysis, structure and kinetics of multimers of different size, overview
Avena sativa
3.2.1.186
More
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
Avena sativa
Synonyms
EC Number
Synonyms
Commentary
Organism
3.2.1.186
aveconasidase
-
Avena sativa
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
3.2.1.21
30
-
assay at
Avena sativa
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.2.1.21
3.9
-
4-nitrophenyl beta-D-glucopyranoside
pH 6.8, 30°C, hexameric enzyme form
Avena sativa
3.2.1.21
29
-
avenacoside
pH 6.8, 30°C, hexameric enzyme form
Avena sativa
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.2.1.21
6.8
-
assay at
Avena sativa
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
3.2.1.21
glucono(1-5)lactone
-
Avena sativa
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.2.1.21
additional information
-
additional information
kinetics of multimers of different size, overview, effects of active site modifcation by N-(dimethylaminopropyl)-N'-ethylcarbodiimide hydrochloride on kinetics, overview
Avena sativa
3.2.1.21
0.063
-
avenacoside
pH 6.8, 30°C, hexameric enzyme form
Avena sativa
3.2.1.21
2.3
-
4-nitrophenyl beta-D-glucopyranoside
pH 6.8, 30°C, hexameric enzyme form
Avena sativa
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.2.1.21
plastid
-
Avena sativa
9536
-
3.2.1.186
plastid
-
Avena sativa
9536
-
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
3.2.1.21
avenacoside + H2O
Avena sativa
the enzyme hydrolyzes the avenacosides to combat fungal attack
C26-desgluco-avenacosides + beta-D-glucose
-
-
?
3.2.1.21
genistin + H2O
Avena sativa
-
?
-
-
?
3.2.1.186
avenacoside A + H2O
Avena sativa
the enzyme in plastid hydrolyzes avenacosides to C26-degluco-avenacosides to combat against fungal infections
26-deglucoavenacoside A + D-glucose
-
-
?
3.2.1.186
avenacoside B + H2O
Avena sativa
the enzyme in plastid hydrolyzes avenacosides to C26-degluco-avenacosides to combat against fungal infections
26-deglucoavenacoside B + D-glucose
-
-
?
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
3.2.1.21
seedling
etiolated
Avena sativa
-
3.2.1.186
leaf
-
Avena sativa
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
3.2.1.21
4-nitrophenyl beta-D-glucopyranoside + H2O
-
666175
Avena sativa
4-nitrophenol + beta-D-glucose
-
-
-
?
3.2.1.21
avenacoside + H2O
-
666175
Avena sativa
C26-desgluco-avenacosides + beta-D-glucose
-
-
-
?
3.2.1.21
avenacoside + H2O
the enzyme hydrolyzes the avenacosides to combat fungal attack
666175
Avena sativa
C26-desgluco-avenacosides + beta-D-glucose
-
-
-
?
3.2.1.21
genistin + H2O
-
666175
Avena sativa
?
-
-
-
?
3.2.1.186
avenacoside A + H2O
-
666175
Avena sativa
26-deglucoavenacoside A + D-glucose
-
-
-
?
3.2.1.186
avenacoside A + H2O
the enzyme in plastid hydrolyzes avenacosides to C26-degluco-avenacosides to combat against fungal infections
666175
Avena sativa
26-deglucoavenacoside A + D-glucose
-
-
-
?
3.2.1.186
avenacoside B + H2O
-
666175
Avena sativa
26-deglucoavenacoside B + D-glucose
-
-
-
?
3.2.1.186
avenacoside B + H2O
the enzyme in plastid hydrolyzes avenacosides to C26-degluco-avenacosides to combat against fungal infections
666175
Avena sativa
26-deglucoavenacoside B + D-glucose
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
3.2.1.21
More
quarternary structure analysis, structure and kinetics of multimers of different size, overview
Avena sativa
3.2.1.186
More
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
Avena sativa
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
3.2.1.21
30
-
assay at
Avena sativa
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.2.1.21
3.9
-
4-nitrophenyl beta-D-glucopyranoside
pH 6.8, 30°C, hexameric enzyme form
Avena sativa
3.2.1.21
29
-
avenacoside
pH 6.8, 30°C, hexameric enzyme form
Avena sativa
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.2.1.21
6.8
-
assay at
Avena sativa