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Literature summary for 3.2.1.3 extracted from
- Purification and properties of a thermoactive glucoamylase from Clostridium thermosacharolyticum (1991), Appl. Environ. Microbiol., 57, 2317-2323.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| beta-cyclodextrins | above 5 mM, slight inhibition | Thermoanaerobacterium thermosaccharolyticum | |
| Cu2+ | - |
Thermoanaerobacterium thermosaccharolyticum |  |
| Pb2+ | - |
Thermoanaerobacterium thermosaccharolyticum | |
| Zn2+ | - |
Thermoanaerobacterium thermosaccharolyticum | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 20 | - |
maltose | - |
Thermoanaerobacterium thermosaccharolyticum | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 75000 | - |
sucrose density gradient centrifugation | Thermoanaerobacterium thermosaccharolyticum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermoanaerobacterium thermosaccharolyticum | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Thermoanaerobacterium thermosaccharolyticum |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 54.4 | - |
- |
Thermoanaerobacterium thermosaccharolyticum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| amylopectin + H2O | - |
Thermoanaerobacterium thermosaccharolyticum | D-glucose + ? | beta-glucose | ? | |
| glycogen + H2O | - |
Thermoanaerobacterium thermosaccharolyticum | glucose + ? | beta-glucose | ? | |
| maltodextrin + H2O | - |
Thermoanaerobacterium thermosaccharolyticum | beta-glucose + ? | - |
? | |
| maltose + H2O | - |
Thermoanaerobacterium thermosaccharolyticum | 2 glucose | - |
? | |
| additional information | enzyme can attack alpha-1,4-glycosidic linkages and alpha-1,6-glycosidic linkages. The velocity of oligosaccharide hydrolysis decreases with a decrease in size of substrate | Thermoanaerobacterium thermosaccharolyticum | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 75000, SDS-PAGE | Thermoanaerobacterium thermosaccharolyticum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
- |
Thermoanaerobacterium thermosaccharolyticum |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | 75 | 50°C: about 40% of maximal activity, 75°C: about 25% of maximal activity | Thermoanaerobacterium thermosaccharolyticum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
- |
Thermoanaerobacterium thermosaccharolyticum |
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Release 2023.1 (January 2023)
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