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Literature summary for 2.1.2.1 extracted from
- Interaction of sheep liver apo-serine hydroxymethyltransferase with pyridoxal-5'-phosphate: a physicochemical, kinetic, and thermodynamic study (1996), Arch. Biochem. Biophys., 330, 363-372.
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 130000 | - |
apoenzyme, peak 2, gel filtration | Ovis aries |
| 200000 | - |
holoenzyme, apoenzyme: peak 1, gel filtration | Ovis aries |
| 213000 | - |
gel filtration | Ovis aries |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Ovis aries | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 52 | - |
apoenzyme, absence of pyridoxal 5'-phosphate | Ovis aries |
| 58 | - |
holoenzyme | Ovis aries |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | 8.3 | stable, at pH 8.55: loss of activity, tetrameric holoenzyme dissociates into the dimeric form, at pH 9.3: complete dissociation | Ovis aries |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis | Ovis aries |  |
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