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Literature summary for 3.2.1.39 extracted from
- Co-purification of glucanase with acid trehalase-invertase aggregate in Saccharomyces cerevisiae (2008), Biotechnol. Lett., 30, 299-304.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | an enzyme deletion strain shows decreased activity of acid trehalase | Saccharomyces cerevisiae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Saccharomyces cerevisiae | role as a regulator for the acid trehalase activity by association in the enzyme aggregate | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
isoform Bgl2 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| isoform Bgl2 copurifies with acid trehalase | Saccharomyces cerevisiae |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 3.5 | - |
pH 4.5, 37°C | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| laminarin + H2O | - |
Saccharomyces cerevisiae | ? | - |
? | |
| additional information | role as a regulator for the acid trehalase activity by association in the enzyme aggregate | Saccharomyces cerevisiae | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 37000-41000, SDS-PAGE | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Bgl2 | isoform | Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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