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Literature summary extracted from
- Crystal structure of GH13 alpha-glucosidase GSJ from one of the deepest sea bacteria (2008), Proteins, 73, 126-133.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.20 | expressed in Bacillus subtilis ISW1214 cells | Geobacillus sp. HTA-462 |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.2.1.20 | crystal structure of the enzyme is determined to a 2.0 A resolution, by X-ray crystallography | Geobacillus sp. HTA-462 |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.20 | D-glucono-1,5-lactone | - |
Geobacillus sp. HTA-462 |  |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.20 | Ca2+ | - |
Geobacillus sp. HTA-462 | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.20 | Geobacillus sp. HTA-462 | Q33E90 | - |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.2.1.20 | glycoprotein | - |
Geobacillus sp. HTA-462 |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.20 | GSJ is purified to homogeneity, gel filtration | Geobacillus sp. HTA-462 |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.20 | oligomaltose + H2O | broad ability in transglycosylation activity on nonsugar acceptors | Geobacillus sp. HTA-462 | D-glucose | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.20 | homodimer | GSJ forms a homodimer under low-ionic strength conditions, while all the structure-determined homologues are supposed to be monomeric proteins | Geobacillus sp. HTA-462 |
| 3.2.1.20 | More | comparisons of the GSJ structure with that of other GH13 enzymes with different catalytic activities reveals that the catalytic cleft of GSJ is widely opened when compared with the homologues | Geobacillus sp. HTA-462 |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.20 | alpha-glucosidase | - |
Geobacillus sp. HTA-462 |
| 3.2.1.20 | GH13 alpha-glucosidase | - |
Geobacillus sp. HTA-462 |
| 3.2.1.20 | GSJ | - |
Geobacillus sp. HTA-462 |
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Release 2023.1 (January 2023)
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