EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.33 | Amine | - |
Oryctolagus cuniculus | |
3.2.1.33 | p-hydroxymercuribenzoate | - |
Oryctolagus cuniculus | |
3.2.1.33 | phosphate | buffer, inhibits at neutral pH | Oryctolagus cuniculus | |
3.2.1.33 | Tris | - |
Oryctolagus cuniculus | |
3.2.1.33 | Urea | - |
Oryctolagus cuniculus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.2.1.33 | 267000 | 279000 | - |
Oryctolagus cuniculus |
3.2.1.33 | 280000 | - |
- |
Saccharomyces cerevisiae |
3.2.1.33 | 280000 | - |
glycogen debranching enzyme, sedimentation equilibrium | Saccharomyces cerevisiae |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.33 | Mammalia | - |
generally present in mammalian tissues | - |
3.2.1.33 | Oryctolagus cuniculus | - |
- |
- |
3.2.1.33 | Saccharomyces cerevisiae | - |
- |
- |
3.2.1.33 | Saccharomyces cerevisiae | - |
baker's yeast | - |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.2.1.33 | liver | - |
Mammalia | - |
3.2.1.33 | liver | - |
Oryctolagus cuniculus | - |
3.2.1.33 | muscle | - |
Mammalia | - |
3.2.1.33 | muscle | - |
Oryctolagus cuniculus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.33 | 63-alpha-glucosyl maltotetraose + H2O | - |
Mammalia | maltotetraose + D-glucose | - |
r | |
3.2.1.33 | 63-alpha-glucosyl maltotetraose + H2O | - |
Oryctolagus cuniculus | maltotetraose + D-glucose | - |
r | |
3.2.1.33 | alpha-(1-6)-glucosyl cyclohexaamylose + H2O | 6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin | Mammalia | cyclohexaamylose + D-glucose | - |
r | |
3.2.1.33 | alpha-(1-6)-glucosyl cyclohexaamylose + H2O | 6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin | Saccharomyces cerevisiae | cyclohexaamylose + D-glucose | - |
r | |
3.2.1.33 | alpha-(1-6)-glucosyl cyclohexaamylose + H2O | 6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin | Oryctolagus cuniculus | cyclohexaamylose + D-glucose | - |
r | |
3.2.1.33 | amylopectin + H2O | - |
Mammalia | amylopectin + D-glucose | - |
? | |
3.2.1.33 | amylopectin + H2O | - |
Saccharomyces cerevisiae | amylopectin + D-glucose | - |
? | |
3.2.1.33 | amylopectin + H2O | - |
Oryctolagus cuniculus | amylopectin + D-glucose | - |
? | |
3.2.1.33 | glycogen + H2O | reverse reaction: incorporation of glucose into glycogen | Mammalia | glycogen + D-glucose | - |
r | |
3.2.1.33 | glycogen + H2O | reverse reaction: incorporation of glucose into glycogen | Saccharomyces cerevisiae | glycogen + D-glucose | - |
r | |
3.2.1.33 | glycogen + H2O | reverse reaction: incorporation of glucose into glycogen | Oryctolagus cuniculus | glycogen + D-glucose | - |
r | |
3.2.1.33 | glycogen + H2O | slight reversibility | Oryctolagus cuniculus | glycogen + D-glucose | - |
r | |
3.2.1.33 | glycogen phosphorylase-limit dextrin + H2O | - |
Saccharomyces cerevisiae | limit dextrin + D-glucose | - |
r | |
3.2.1.33 | glycogen phosphorylase-limit dextrin + H2O | phi-dextrin | Mammalia | limit dextrin + D-glucose | - |
r | |
3.2.1.33 | glycogen phosphorylase-limit dextrin + H2O | phi-dextrin | Saccharomyces cerevisiae | limit dextrin + D-glucose | - |
r | |
3.2.1.33 | glycogen phosphorylase-limit dextrin + H2O | phi-dextrin | Oryctolagus cuniculus | limit dextrin + D-glucose | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.2.1.33 | trimer | - |
Saccharomyces cerevisiae |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.33 | amyloglucosidase | - |
Mammalia |
3.2.1.33 | amyloglucosidase | - |
Saccharomyces cerevisiae |
3.2.1.33 | amyloglucosidase | - |
Oryctolagus cuniculus |
3.2.1.33 | glycogen debranching system | EC 3.2.1.33 found in mammals and yeast is in a single polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25, 4-alpha-glucanotransferase, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can hydrolyse. Together, these two activities constitute the glycogen debranching system | Mammalia |
3.2.1.33 | glycogen debranching system | EC 3.2.1.33 found in mammals and yeast is in a single polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25, 4-alpha-glucanotransferase, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can hydrolyse. Together, these two activities constitute the glycogen debranching system | Saccharomyces cerevisiae |
3.2.1.33 | glycogen debranching system | EC 3.2.1.33 found in mammals and yeast is in a single polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25, 4-alpha-glucanotransferase, which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-alpha-glucosidase activity can hydrolyse. Together, these two activities constitute the glycogen debranching system | Oryctolagus cuniculus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.33 | additional information | - |
pH-optimum depends on type of buffer | Oryctolagus cuniculus |
3.2.1.33 | additional information | - |
2 enzymes: one with an acid and one with a neutral pH-optimum | Oryctolagus cuniculus |
3.2.1.33 | 6 | - |
substrate: glycogen phosphorylase limit dextrin, citrate /phosphate buffer | Oryctolagus cuniculus |
3.2.1.33 | 6 | 6.6 | - |
Saccharomyces cerevisiae |
3.2.1.33 | 6.6 | - |
- |
Oryctolagus cuniculus |
3.2.1.33 | 7.2 | - |
- |
Oryctolagus cuniculus |
3.2.1.33 | 7.6 | - |
citrate buffer | Oryctolagus cuniculus |