EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.2.1.33 | 5,5'-dithiobis(2-nitrobenzoic acid) | DTNB | Oryctolagus cuniculus | |
3.2.1.33 | 5-amino-D-glucose | nojirimycin, potent inhibitor, noncompetitive | Oryctolagus cuniculus | |
3.2.1.33 | maltotriose | competitive | 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 | |
3.2.1.33 | additional information | - |
additional information | kinetic mechanism | 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 | |
3.2.1.33 | 6-O-alpha-D-glucosyl cyclomaltoheptaose + H2O = D-glucose + cyclomaltoheptaose | thermodynamic data | Oryctolagus cuniculus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.2.1.33 | muscle | skeletal | 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 | 63-alpha-glucosyl maltotetraose + H2O | branched pentasaccharide "fast B5" | Oryctolagus cuniculus | maltotetraose + 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 | glycogen + H2O | reverse reaction: incorporation of glucose into glycogen | 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 | Subunits | Comment | Organism |
---|---|---|---|
3.2.1.33 | monomer | - |
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 |