Inhibitors | Comment | Organism | Structure |
---|---|---|---|
1,4-diaminobutane | putrescine, glycogen debranching enzyme, slight inhibition | Oryctolagus cuniculus | |
2,2-bis(hydroxymethyl)-2,2',2''-nitrilotriethanol | Bis-Tris, reversible inhibitor; noncompetitive with glycogen phosphorylase limit dextrin, competitive with glucose | Oryctolagus cuniculus | |
2-(2-hydroxyethylamino)-2-hydroxymethyl-1,3-propanediol | hydroxyethyltris | Oryctolagus cuniculus | |
2-amino-1,3-propandiol | - |
Oryctolagus cuniculus | |
2-amino-2-methyl-1,3-propanediol | - |
Oryctolagus cuniculus | |
2-hydroxyethyl-3-hydroxypropylamine | HEPA, glycogen debranching enzyme | Oryctolagus cuniculus | |
3-aminopropyl-2-hydroxyethylamine | DAPH, glycogen debranching enzyme | Oryctolagus cuniculus | |
5-amino-D-glucose | nojirimycin, potent inhibitor, noncompetitive | Oryctolagus cuniculus | |
5-thio-D-glucose | slight inhibition | Oryctolagus cuniculus | |
Amine | noncompetitive with glycogen phosphorylase limit dextrin, competitive with glucose; polyhydroxyamines, mechanism of inhibition; protonated, hydroxylalkyl-substituted, noncompetitive, mechanism of inhibition | Oryctolagus cuniculus | |
cyclohexaamylose | alpha-Schardinger dextrin, debranching enzyme, competitive inhibitor | Oryctolagus cuniculus | |
D-glucono-1,5-lactone | glycogen debranching enzyme, noncompetitive with glycogen phosphorylase limit dextrin, competitive with glucose | Oryctolagus cuniculus | |
ethylamine | slight inhibition | Oryctolagus cuniculus | |
glycogen | competitive | Oryctolagus cuniculus | |
m-erythritol | noncompetitive | Oryctolagus cuniculus | |
additional information | inhibition mechanism; no inhibition by dithioerythritol, dithiothreitol, cadaverine, spermidine, spermine, D,L-threitol, 1-thio-beta-D-glucose | Oryctolagus cuniculus | |
N,N'-bis(tris[hydroxymethyl]methyl)-1,3-diaminopropane | bis(tris)propane, noncompetitive | Oryctolagus cuniculus | |
Tris | noncompetitive; Tris analogues | Oryctolagus cuniculus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic data | Oryctolagus cuniculus | |
additional information | - |
additional information | kinetic mechanism | Oryctolagus cuniculus | |
43 | - |
D-glucose | - |
Oryctolagus cuniculus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
160000 | 170000 | - |
Oryctolagus cuniculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
glycogen phosphorylase-limit dextrin + H2O | Oryctolagus cuniculus | phi-dextrin | ? | - |
? | |
glycogen phosphorylase-limit dextrin + H2O | Oryctolagus cuniculus | total degradation of glycogen is accomplished by the combined action of glycogen phosphorylase and glycogen debranching enzyme | ? | - |
? |
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 | thermodynamic data | Oryctolagus cuniculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
muscle | skeletal | Oryctolagus cuniculus | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
6.5 | 8.9 | - |
Oryctolagus cuniculus |
Storage Stability | Organism |
---|---|
4°C, 50 mM Tris, 5 mM EDTA, 1 mM dithiothreitol, pH 7.2 | Oryctolagus cuniculus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
63-alpha-glucosyl maltotetraose + H2O | branched pentasaccharide "fast B5" | Oryctolagus cuniculus | maltotetraose + D-glucose | - |
r | |
alpha-(1-6)-glucosyl cyclohexaamylose + H2O | 6-alpha-glucosyl alpha-Schardinger dextrin, cyclodextrin | Oryctolagus cuniculus | cyclohexaamylose + D-glucose | - |
r | |
glycogen + H2O | slowly hydrolyzed | Oryctolagus cuniculus | glycogen + D-glucose | - |
r | |
glycogen + H2O | reverse reaction: incorporation of glucose into glycogen | Oryctolagus cuniculus | glycogen + D-glucose | - |
r | |
glycogen phosphorylase-limit dextrin + H2O | phi-dextrin | Oryctolagus cuniculus | limit dextrin + D-glucose | - |
r | |
glycogen phosphorylase-limit dextrin + H2O | phi-dextrin | Oryctolagus cuniculus | ? | - |
? | |
glycogen phosphorylase-limit dextrin + H2O | total degradation of glycogen is accomplished by the combined action of glycogen phosphorylase and glycogen debranching enzyme | Oryctolagus cuniculus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | - |
Oryctolagus cuniculus |
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 |