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Literature summary extracted from
- Resolution, purification, characterization of two extracellular glucohydrolases, alpha-glucosidase and maltase, of Bacillus licheniformis (1986), Can. J. Microbiol., 32, 342-347.
No PubMed abstract available
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.20 | D-glucono-delta-lactone | - |
Bacillus licheniformis |  |
| 3.2.1.20 | D-glucose | alpha-glucosidase is inhibited to a far greater extent than maltase | Bacillus licheniformis | |
| 3.2.1.20 | Tris | - |
Bacillus licheniformis | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.2.1.20 | extracellular | - |
Bacillus licheniformis | - |
- |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | 40000 | - |
x * 40000 + x * 60000, maltase, SDS-PAGE | Bacillus licheniformis |
| 3.2.1.20 | 60000 | - |
x * 40000 + x * 60000, maltase, SDS-PAGE | Bacillus licheniformis |
| 3.2.1.20 | 63000 | - |
1 * 63000, alpha-glucosidase, SDS-PAGE | Bacillus licheniformis |
| 3.2.1.20 | 66000 | - |
alpha-glucosidase, gel filtration | Bacillus licheniformis |
| 3.2.1.20 | 160000 | - |
maltase, gel filtration | Bacillus licheniformis |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.20 | Bacillus licheniformis | - |
resolution of the alpha-glucosidase system into two enzymes: alpha-glucosidase and maltase | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.20 | - |
Bacillus licheniformis |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | additional information | - |
- |
Bacillus licheniformis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.20 | isomaltose + H2O | low activity | Bacillus licheniformis | 2 alpha-D-glucose | - |
? | |
| 3.2.1.20 | isomaltose + H2O | maltase shows low activity with isomaltose, alpha-glucosidase shows high activity | Bacillus licheniformis | 2 alpha-D-glucose | - |
? | |
| 3.2.1.20 | maltose + H2O | maltase hydrolyzes maltose preferentially | Bacillus licheniformis | alpha-D-glucose + D-glucose | - |
? | |
| 3.2.1.20 | additional information | maltase shows no transglucosylation activity, alpha-glucosidase shows transglucosidase activity with isomaltose or maltotriose | Bacillus licheniformis | ? | - |
? | |
| 3.2.1.20 | p-nitrophenyl-alpha-D-glucopyranoside + H2O | p-nitrophenyl-alpha-D-glucopyranoside | Bacillus licheniformis | 4-nitrophenol + D-glucose | - |
? | |
| 3.2.1.20 | p-nitrophenyl-alpha-D-glucopyranoside + H2O | maltase shows low activity with p-nitrophenyl-alpha-D-glucopyranoside, alpha-glucosidase shows high activity | Bacillus licheniformis | 4-nitrophenol + D-glucose | - |
? | |
| 3.2.1.20 | sucrose + H2O | - |
Bacillus licheniformis | D-fructose + alpha-D-glucose | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.20 | ? | x * 40000 + x * 60000, maltase, SDS-PAGE | Bacillus licheniformis |
| 3.2.1.20 | monomer | 1 * 63000, alpha-glucosidase, SDS-PAGE | Bacillus licheniformis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | 40 | - |
- |
Bacillus licheniformis |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | 30 | 60 | 30°C, 60% of maltase activity, 88% of alpha-glucosidase activity, 60°C: no maltase activity, 8% of alpha-glucosidase activity | Bacillus licheniformis |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | 4 | - |
60 min, maltase activity and alpha-glucosidase activity, stable | Bacillus licheniformis |
| 3.2.1.20 | 20 | - |
60 min, maltase activity and alpha-glucosidase activity, stable | Bacillus licheniformis |
| 3.2.1.20 | 30 | - |
60 min, maltase activity and alpha-glucosidase activity, stable | Bacillus licheniformis |
| 3.2.1.20 | 50 | - |
60 min, complete inactivation of maltase, alpha-glucosidase loses 86% of its activity | Bacillus licheniformis |
| 3.2.1.20 | 60 | - |
10 min, complete loss of maltase activity and alpha-glucosidase activity | Bacillus licheniformis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | 6 | - |
alpha-glucosidase activity and maltase activity | Bacillus licheniformis |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | 5 | 7 | about 70% of activity at pH 5.5 and pH 6.5, maltase and alpha-glucosidase | Bacillus licheniformis |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.20 | 9 | - |
alpha-glucosidase remains fairly stable, maltase retains only 10% of its activity | Bacillus licheniformis |
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