Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Tris | - |
Oryctolagus cuniculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
glycogen debranching enzyme | Oryctolagus cuniculus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O = D-glucose + cyclomaltoheptaose | mechanism | Oryctolagus cuniculus | |
6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O = D-glucose + cyclomaltoheptaose | alpha-(1->6) linkage can be synthesized in the absence of polysaccharide | Oryctolagus cuniculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
muscle | - |
Oryctolagus cuniculus | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
6.5 | 8.3 | - |
Oryctolagus cuniculus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 D-glucose | - |
Oryctolagus cuniculus | 6-O-alpha-D-glucosyl-D-glucose + H2O | isomaltose | r | |
63-alpha-glucosyl maltotetraose + H2O | branched pentasaccharide "fast B5" | Oryctolagus cuniculus | maltotetraose + D-glucose | - |
r | |
alpha-(1-6)-glucosyl cyclohexaamylose + H2O | - |
Oryctolagus cuniculus | cyclohexaamylose + D-glucose | - |
r | |
glycogen + H2O | reverse reaction: synthesis of (1, 6)-bound side chains, reincorporation of glucose into polysaccharide | Oryctolagus cuniculus | glycogen + D-glucose | - |
r | |
glycogen phosphorylase-limit dextrin + H2O | - |
Oryctolagus cuniculus | limit dextrin + D-glucose | - |
r |
Synonyms | Comment | Organism |
---|---|---|
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 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
pH-optimum depends on type of buffer | Oryctolagus cuniculus |
additional information | - |
pH optimum is the same in both degradative and synthetic directions and optimum is shifted and inhibited by Tris in the same manner in both directions | Oryctolagus cuniculus |
6.6 | - |
anionic buffer, substrate: glycogen phosphorylase limit dextrin | Oryctolagus cuniculus |
7.2 | - |
cationic buffer, substrate: glycogen phosphorylase limit dextrin | Oryctolagus cuniculus |