EC Number   |
pH Stability |
pH Stability Maximum |
Reference |
|---|
    2.1.2.1 | -999 |
- |
recombinant wild-type bsSHMT and chimeric mutant enzyme are significantly higher susceptible to proteolysis into smaller protein fragments at pH 11 as compared to neutral pH |
718968 |
| 2.1.2.1 | -999 |
- |
recombinant wild-type bstSHMT and chimeric mutant enzyme are only merginally susceptible to proteolysis into smaller protein fragments at pH 11 and at neutral pH |
718968 |
| 2.1.2.1 | 2 |
7 |
the enzyme retains more than 50% of its activity after 30 min at pH 2.0-7.0 |
755905 |
| 2.1.2.1 | 5.5 |
8.5 |
the enzyme retains over 80% of the maximum activity over a pH range from 7.0 to 8.5 for 24 h at 4°C, and more than 70% of the maximal activity at pH 6.5. However, the enzyme exhibits a rapid decrease in activity at pH 5.5 |
756288 |
| 2.1.2.1 | 5.5 |
9 |
purified recombinant SaSHMT shows significant stability under weakly acidic and alkaline environment at pH 6.5-9.0. Without any stabilizer at pH 6.5-9.0 for 96 h at 4°C over 80% of maximum activity is retained, at pH 5.5-6.0 less than 80% activity remains, the enzyme is unstable below pH 5.5 |
736753 |
| 2.1.2.1 | 5.8 |
8.5 |
stable, rabbit cytosol |
441420 |
| 2.1.2.1 | 6 |
7.5 |
stable |
441410 |
| 2.1.2.1 | 6 |
8 |
purified recombinant enzyme, over 60% maximal activity remains after 24 h at pH 6.0-7.5, 4°C, less than 20% of maximal activity at pH 8.0 |
736645 |
| 2.1.2.1 | 6 |
8.5 |
stable |
441412 |
| 2.1.2.1 | 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 |
441426 |
