EC Number   |
Subunits |
Reference  |
|---|
   3.4.19.3 | trimer |
3 * 24000, SDS-PAGE |
95280, 95290 |
| 3.4.19.3 | tetramer |
4 * 23500, SDS-PAGE |
95294 |
| 3.4.19.3 | dimer |
2 * 22441, calculation from nucleotide sequence |
95295 |
| 3.4.19.3 | dimer |
2 * 23000, SDS-PAGE |
95295 |
| 3.4.19.3 | monomer |
1 * 24000, SDS-PAGE |
681896, 95296 |
| 3.4.19.3 | tetramer |
4 * 25200, SDS-PAGE |
95303 |
| 3.4.19.3 | ? |
x * 23135, calculation from nucleotide sequence |
95307 |
| 3.4.19.3 | ? |
x * 23777, calculation from nucleotide sequence |
95308 |
| 3.4.19.3 | ? |
x * 30000, wild-type enzyme, 3 bands of 30000 Da and of 60000 Da are detected in mutant enzymes S185C and C68S/S185C, SDS-PAGE in presence and in absence of 2-mercaptoethanol |
650352 |
| 3.4.19.3 | dimer |
the mutant enzyme C142S/C188S is tetrameric above pH 4. The fraction of the dimeric form increases with increasing acidity below pH 4 and then the protein dissociates completely into a monomeric form at pH 2.5 |
651099 |
