Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | the deglycosylated enzyme is more sensitive to proteolytic degradation by subtilisin than the native enzyme | Aspergillus niger |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.1 | - |
starch | pH 4.8, 37°C, deglycosylated enzyme | Aspergillus niger | |
1.2 | - |
starch | pH 4.8, 37°C, native enzyme | Aspergillus niger |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus niger | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | effects of deglycosylation on enzyme structure, activity and stability, overview, deglycosylation by alpha-mannosidase does not affect the pH optimum or the active site and catalytic reaction mechanism including conformational changes of the enzyme, the secondary enzyme structure remains unaltered, deglycosylation increases the enzyme aggregation and reduces the thermal stability, the deglycosylated enzyme is more sensitive to proteolytic degradation by subtilisin than the native enzyme | Aspergillus niger |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Aspergillus niger | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
starch + H2O | - |
Aspergillus niger | starch + beta-D-glucose | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | structure-function relationship analysis | Aspergillus niger |
Synonyms | Comment | Organism |
---|---|---|
GA | - |
Aspergillus niger |
glucoamylase | - |
Aspergillus niger |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at room temperature | Aspergillus niger |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
the deglycosylated enzyme shows a higher aggregation rate compared to the native enzyme dependent on pH and presence of divalent cations, e.g. Mg2+ or Ca2+ | Aspergillus niger |
60 | 80 | the thermal stability at 70°C and other temperatures of the deglycosylated enzyme is reduced compared to the native enzyme | Aspergillus niger |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
4.8 | - |
native and deglycosylated enzyme | Aspergillus niger |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Aspergillus niger | - |
3.7 | 3.5 |