EC Number   |
pH Stability |
pH Stability Maximum |
Reference |
|---|
   3.4.14.9 | 2 |
5 |
optimal activation occurs in the range pH 3.0-4.0, the proteolytic processing takes place in a wider pH range (2.0-5.0), at pH 3.0 and lower, TPP I is quickly inactivated, whereas the polypeptide generated at higher pH (4.5-5.0) possesses 6- and 13-aa N-terminal extensions and is inactive, the enzyme is unstable at alkaline and neutral pH |
678513 |
| 3.4.14.9 | 2.5 |
5 |
stable |
665428 |
| 3.4.14.9 | 3 |
- |
has weak endoproteolytic activity at pH 3 |
678398 |
| 3.4.14.9 | 3 |
6 |
at pH 3.0 the activity of TPP I is less than 75% of its maximal activity at pH 4.5, most stable at pH 3-4, no activity at pH above 6.0 |
679200 |
| 3.4.14.9 | 3.5 |
- |
TPP I is an acidic protease that is quickly inactivated under alkaline pH conditions, in the absence of prosegment, the enzyme is quickly denatured with a rate constant of around 0.107/min, amounting to a half-life of 6.472 min, whereas in the presence of the prosegment, the inactivation rate is reduced to about 0.035/min, and approximately 84% of the activity is preserved after over 2 h of incubation |
698756 |
| 3.4.14.9 | 3.5 |
4.5 |
stable |
647183 |
| 3.4.14.9 | 5 |
6 |
48 h, stable |
647186 |
| 3.4.14.9 | 7 |
- |
48 h, unstable above |
647186 |
| 3.4.14.9 | 7.4 |
- |
37°C, half-life: of mature enzyme in absence of heparin is 2.5 min, of mature enzyme in presence of heparin is 21.5 min |
665697 |
