Any feedback?
Literature summary for 3.2.1.33 extracted from
- Preparation and properties of the glycogen-debranching enzyme from rabbit liver (1972), Biochim. Biophys. Acta, 289, 97-107.
General Stability
| General Stability | Organism |
|---|---|
| stable in 2 M urea, irreversible denaturation with higher concentrations, 3 M, of urea | Oryctolagus cuniculus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| guanidine | at 0.05 M: 20% inhibition, at 0.15 M: 50% inhibition | Oryctolagus cuniculus |  |
| imidazole | buffer, 50% inhibition | Oryctolagus cuniculus | |
| Tris | buffer, strong inhibition | Oryctolagus cuniculus | |
| Urea | muscle enzyme: reversible 95% inhibition by 2 M urea, with higher concentration, 3 M urea: time-dependent irreversible denaturation, liver enzyme: reversible 57% inhibition by 2 M urea; reversible inhibitor below 2 M, 90% inhibition by 2.6 M urea | Oryctolagus cuniculus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 179300 | - |
glycogen debranching enzyme, liver enzyme, sucrose density gradient centrifugation | Oryctolagus cuniculus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Oryctolagus cuniculus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| glycogen debranching enzyme | Oryctolagus cuniculus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Oryctolagus cuniculus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 4.5 | - |
liver enzyme | Oryctolagus cuniculus |
| 5.86 | - |
- |
Oryctolagus cuniculus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 63-alpha-glucosyl maltotetraose + H2O | branched pentasaccharide "fast B5" | Oryctolagus cuniculus | maltotetraose + D-glucose | - |
r | |
| 63-alpha-maltotriosyl maltotetraose + H2O | branched heptasaccharide B7 | Oryctolagus cuniculus | ? | - |
? | |
| glycogen phosphorylase-limit dextrin + H2O | - |
Oryctolagus cuniculus | limit dextrin + D-glucose | - |
r | |
Synonyms
| 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
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
pH-optimum depends on type of buffer | Oryctolagus cuniculus |
| 5.4 | - |
imidazole buffer, about 50% inhibition | Oryctolagus cuniculus |
| 6 | - |
substrate: glycogen phosphorylase limit dextrin, citrate /phosphate buffer | Oryctolagus cuniculus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 8 | - |
Oryctolagus cuniculus |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0015 | - |
guanidine | - |
Oryctolagus cuniculus | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
