General Stability | Organism |
---|---|
trypsin hydrolysis releases polypeptides containing the alpha-glucosidase I catalytic domain, with no loss of catalytic activity | Saccharomyces cerevisiae |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
98000 | - |
SDS-PAGE | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Saccharomyces cerevisiae | regulates one of the key steps in asparagines-linked glycoprotein biosynthesis | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Purification (Comment) | Organism |
---|---|
soluble form | Saccharomyces cerevisiae |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
3130 | - |
- |
Saccharomyces cerevisiae |
Storage Stability | Organism |
---|---|
storage of the partially purified protein for 1 month at 4°C results in complete loss of the 98000 Da band, but the enzymatic activity remains, suggesting that either one or several of the peptides contain an active catalytic fragment that is resistant to further degradation | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Glc3Man9GlcNAc2 + H2O | hydrolyses specifically terminal alpha1,2-linked glucose residue | Saccharomyces cerevisiae | D-glucose + Glc2Man9GlcNAc2 | - |
? | |
additional information | regulates one of the key steps in asparagines-linked glycoprotein biosynthesis | Saccharomyces cerevisiae | ? | - |
? |