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Literature summary extracted from
- Characterization of novel thermophilic alpha-glucosidase from Bifidobacterium longum (2017), Int. J. Biol. Macromol., 99, 594-599 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.20 | expressed in Escherichia coli MC1061 cells | Bifidobacterium longum subsp. Longum |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.20 | Ca2+ | 48% residual activity at 5 mM | Bifidobacterium longum subsp. Longum |  |
| 3.2.1.20 | Co2+ | 47% residual activity at 5 mM | Bifidobacterium longum subsp. Longum | |
| 3.2.1.20 | Fe2+ | complete inhibition at 5 mM | Bifidobacterium longum subsp. Longum | |
| 3.2.1.20 | additional information | not inhibited by EDTA | Bifidobacterium longum subsp. Longum |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.20 | 1.8 | - |
4-nitrophenyl alpha-D-glucoside | at pH 6.5 and 65°C | Bifidobacterium longum subsp. Longum | |
| 3.2.1.20 | 2.6 | - |
maltotriose | at pH 6.5 and 65°C | Bifidobacterium longum subsp. Longum | |
| 3.2.1.20 | 29.6 | - |
isomaltose | at pH 6.5 and 65°C | Bifidobacterium longum subsp. Longum | |
| 3.2.1.20 | 43.5 | - |
maltose | at pH 6.5 and 65°C | Bifidobacterium longum subsp. Longum | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.20 | additional information | not affected by Mg2+, Cu2+, Mn2+ and Zn2+ | Bifidobacterium longum subsp. Longum |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.20 | Bifidobacterium longum subsp. Longum | - |
- |
- |
| 3.2.1.20 | Bifidobacterium longum subsp. Longum JCM1217 | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.20 | Ni-NTA column chromatography | Bifidobacterium longum subsp. Longum |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.20 | 4-nitrophenyl alpha-D-glucoside + H2O | - |
Bifidobacterium longum subsp. Longum | 4-nitrophenol + alpha-D-glucose | - |
? | |
| 3.2.1.20 | isomaltose + H2O | - |
Bifidobacterium longum subsp. Longum | alpha-D-glucose + D-glucose | - |
? | |
| 3.2.1.20 | isomaltose + H2O | - |
Bifidobacterium longum subsp. Longum JCM1217 | alpha-D-glucose + D-glucose | - |
? | |
| 3.2.1.20 | kojibiose + H2O | - |
Bifidobacterium longum subsp. Longum | alpha-D-glucose + D-glucose | - |
? | |
| 3.2.1.20 | kojibiose + H2O | - |
Bifidobacterium longum subsp. Longum JCM1217 | alpha-D-glucose + D-glucose | - |
? | |
| 3.2.1.20 | maltose + H2O | - |
Bifidobacterium longum subsp. Longum | alpha-D-glucose + D-glucose | - |
? | |
| 3.2.1.20 | maltose + H2O | - |
Bifidobacterium longum subsp. Longum JCM1217 | alpha-D-glucose + D-glucose | - |
? | |
| 3.2.1.20 | maltotetraose + H2O | - |
Bifidobacterium longum subsp. Longum | alpha-D-glucose + ? | - |
? | |
| 3.2.1.20 | maltotriose + H2O | - |
Bifidobacterium longum subsp. Longum | alpha-D-glucose + ? | - |
? | |
| 3.2.1.20 | maltotriose + H2O | highest activity | Bifidobacterium longum subsp. Longum | alpha-D-glucose + ? | - |
? | |
| 3.2.1.20 | additional information | the enzyme is able to hydrolyze alpha-1,2, alpha-1,3, alpha-1,4, and alpha-1,6 glycosidic O-linkages and liberates alpha-D-glucose from the non-reducing end of substrates | Bifidobacterium longum subsp. Longum | ? | - |
? | |
| 3.2.1.20 | additional information | the enzyme is not able to hydrolyze polysaccharides, such as amylose, amylopectin, starch, or alpha-, beta-, and gamma-cyclodextrin | Bifidobacterium longum subsp. Longum | ? | - |
? | |
| 3.2.1.20 | additional information | the enzyme is able to hydrolyze alpha-1,2, alpha-1,3, alpha-1,4, and alpha-1,6 glycosidic O-linkages and liberates alpha-D-glucose from the non-reducing end of substrates | Bifidobacterium longum subsp. Longum JCM1217 | ? | - |
? | |
| 3.2.1.20 | additional information | the enzyme is not able to hydrolyze polysaccharides, such as amylose, amylopectin, starch, or alpha-, beta-, and gamma-cyclodextrin | Bifidobacterium longum subsp. Longum JCM1217 | ? | - |
? | |
| 3.2.1.20 | nigerose + H2O | - |
Bifidobacterium longum subsp. Longum | alpha-D-glucose + ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.20 | ? | x * 67000, SDS-PAGE | Bifidobacterium longum subsp. Longum |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.20 | alpha-D-glucoside glucohydrolase | - |
Bifidobacterium longum subsp. Longum |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | 75 | - |
- |
Bifidobacterium longum subsp. Longum |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | 50 | 55 | the enzyme activity decreases significantly at temperatures below 55°C, and about 80% of the catalytic activity is lost at 50°C | Bifidobacterium longum subsp. Longum |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.20 | 5 | - |
maltose | at pH 6.5 and 65°C | Bifidobacterium longum subsp. Longum | |
| 3.2.1.20 | 9.3 | - |
isomaltose | at pH 6.5 and 65°C | Bifidobacterium longum subsp. Longum | |
| 3.2.1.20 | 103.6 | - |
maltotriose | at pH 6.5 and 65°C | Bifidobacterium longum subsp. Longum | |
| 3.2.1.20 | 371 | - |
4-nitrophenyl alpha-D-glucoside | at pH 6.5 and 65°C | Bifidobacterium longum subsp. Longum | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | 7.5 | - |
in maleic acid Tris-NaOH | Bifidobacterium longum subsp. Longum |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | 6 | 8 | more than 60% activity between pH 6.0 and 8.0 in maleic acid Tris-NaOH | Bifidobacterium longum subsp. Longum |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.20 | 0.1 | - |
maltose | at pH 6.5 and 65°C | Bifidobacterium longum subsp. Longum | |
| 3.2.1.20 | 0.1 | - |
isomaltose | at pH 6.5 and 65°C | Bifidobacterium longum subsp. Longum | |
| 3.2.1.20 | 4.5 | - |
maltotetraose | at pH 6.5 and 65°C | Bifidobacterium longum subsp. Longum | |
| 3.2.1.20 | 12.1 | - |
nigerose | at pH 6.5 and 65°C | Bifidobacterium longum subsp. Longum | |
| 3.2.1.20 | 39.8 | - |
maltotriose | at pH 6.5 and 65°C | Bifidobacterium longum subsp. Longum | |
| 3.2.1.20 | 206.1 | - |
4-nitrophenyl alpha-D-glucoside | at pH 6.5 and 65°C | Bifidobacterium longum subsp. Longum | |
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