EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.33 | alpha-cyclodextrin | 20 mM: 2.3fold activation | Oryctolagus cuniculus | |
3.2.1.33 | amylopectin | potent activator | Oryctolagus cuniculus | |
3.2.1.33 | glucooligosaccharides | with four or more glucose units, uncompetitive activation | Oryctolagus cuniculus | |
3.2.1.33 | glycogen | potent activator | Oryctolagus cuniculus | |
3.2.1.33 | maltohexaose | 20 mM: 1.86fold activation | Oryctolagus cuniculus | |
3.2.1.33 | maltopentaose | 20 mM: 1.45fold activation | Oryctolagus cuniculus | |
3.2.1.33 | maltotetraose | 20 mM: 1.15fold activation | Oryctolagus cuniculus | |
3.2.1.33 | additional information | mechanism of activation | Oryctolagus cuniculus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.33 | D-glucose | competitive | Oryctolagus cuniculus | |
3.2.1.33 | glucooligosaccharides | containing one, two, or three glucose, competitive inhibitors | Oryctolagus cuniculus | |
3.2.1.33 | maltose | competitive | Oryctolagus cuniculus | |
3.2.1.33 | maltotriose | competitive | Oryctolagus cuniculus | |
3.2.1.33 | additional information | inhibition mechanism | Oryctolagus cuniculus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.33 | additional information | - |
additional information | kinetic data | Oryctolagus cuniculus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.33 | glycogen phosphorylase-limit dextrin + H2O | Oryctolagus cuniculus | - |
? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.33 | Oryctolagus cuniculus | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.33 | glycogen debranching enzyme | Oryctolagus cuniculus |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.2.1.33 | 6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O = D-glucose + cyclomaltoheptaose | mechanism | Oryctolagus cuniculus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.2.1.33 | muscle | - |
Oryctolagus cuniculus | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.2.1.33 | 11 | - |
- |
Oryctolagus cuniculus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.33 | alpha-D-glucosyl fluoride | - |
Oryctolagus cuniculus | fluoride + D-glucose | - |
? | |
3.2.1.33 | glycogen + H2O | slowly hydrolyzed | Oryctolagus cuniculus | glycogen + D-glucose | - |
r | |
3.2.1.33 | glycogen phosphorylase-limit dextrin + H2O | - |
Oryctolagus cuniculus | limit dextrin + D-glucose | - |
r | |
3.2.1.33 | glycogen phosphorylase-limit dextrin + H2O | - |
Oryctolagus cuniculus | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
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 |