Any feedback?
Literature summary extracted from
- Novel type of enzyme multimerization enhances substrate affinity of oat beta-glucosidase (2005), J. Struct. Biol., 150, 1-10.
Inhibitors
| EC Number | Inhibitors | Comment | 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 | Comment | 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 | Comment | 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 | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 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 | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.21 | Avena sativa | - |
type I enzyme | - |
| 3.2.1.186 | Avena sativa | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.2.1.21 | seedling | etiolated | Avena sativa | - |
| 3.2.1.186 | leaf | - |
Avena sativa | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.21 | 4-nitrophenyl beta-D-glucopyranoside + H2O | - |
Avena sativa | 4-nitrophenol + beta-D-glucose | - |
? | |
| 3.2.1.21 | avenacoside + H2O | - |
Avena sativa | C26-desgluco-avenacosides + beta-D-glucose | - |
? | |
| 3.2.1.21 | avenacoside + H2O | the enzyme hydrolyzes the avenacosides to combat fungal attack | Avena sativa | C26-desgluco-avenacosides + beta-D-glucose | - |
? | |
| 3.2.1.21 | genistin + H2O | - |
Avena sativa | ? | - |
? | |
| 3.2.1.186 | avenacoside A + H2O | - |
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 | Avena sativa | 26-deglucoavenacoside A + D-glucose | - |
? | |
| 3.2.1.186 | avenacoside B + H2O | - |
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 | Avena sativa | 26-deglucoavenacoside B + D-glucose | - |
? | |
Subunits
| EC Number | Subunits | Comment | 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 | Comment | Organism |
|---|---|---|---|
| 3.2.1.186 | aveconasidase | - |
Avena sativa |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | 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 | Comment | 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 | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.21 | 6.8 | - |
assay at | Avena sativa |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
