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Literature summary extracted from
- Purification, properties and structural aspects of a thermoacidophilic alpha-amylase from Alicyclobacillus acidocaldarius ATCC 27009. Insight into acidostability of proteins (1994), Eur. J. Biochem., 226, 981-991.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.1 | expression in Escherichia coli | Alicyclobacillus acidocaldarius |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.2.1.1 | extracellular | - |
Alicyclobacillus acidocaldarius | - |
- |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 160000 | - |
x * 160000, SDS-PAGE | Alicyclobacillus acidocaldarius |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.1 | Alicyclobacillus acidocaldarius | - |
ATCC 27009 | - |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.2.1.1 | glycoprotein | carbohydrate is O-glycosidically linked to the protein, the carbohydrate moiety is confined to the region N-terminal to Asp466 or C-terminal to approximately residue 1200 | Alicyclobacillus acidocaldarius |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.1 | - |
Alicyclobacillus acidocaldarius |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.2.1.1 | culture medium | - |
Alicyclobacillus acidocaldarius | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 16.9 | - |
- |
Alicyclobacillus acidocaldarius |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.1 | pullulan + H2O | - |
Alicyclobacillus acidocaldarius | panose + ? | - |
? |  |
| 3.2.1.1 | starch + H2O | - |
Alicyclobacillus acidocaldarius | additional information | maltotriose + maltose, glucose is also formed | ? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.1 | ? | x * 160000, SDS-PAGE | Alicyclobacillus acidocaldarius |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 75 | - |
- |
Alicyclobacillus acidocaldarius |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 60 | 80 | 60°C: about 40% of maximal activity, 80°C: about 90% of maximal activity, 85°C: about 20% of maximal activity | Alicyclobacillus acidocaldarius |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 3 | - |
- |
Alicyclobacillus acidocaldarius |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 1.2 | 6 | pH 1.2: about 40% of maximal activity, pH 6.0: about 50% of maximal activity | Alicyclobacillus acidocaldarius |
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Release 2023.1 (January 2023)
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