EC Number   |
Subunits |
Reference |
|---|
   2.4.1.4 | ? |
x * 32700, SDS-PAGE |
-, 735570 |
| 2.4.1.4 | ? |
x * 72466, sequence calculation, excluding the transit peptide, x * 85000, about, recombinant SBD-fusion enzyme, SDS-PAGE |
737050 |
| 2.4.1.4 | ? |
x * 73000, recombinant His6-tagged enzyme, SDS-PAGE |
718673 |
| 2.4.1.4 | ? |
x * 73214, sequence calculation, x * 73000, recombinant detagged enzyme, SDS-PAGE |
721111 |
| 2.4.1.4 | dimer |
- |
-, 756235, 756762, 756947 |
| 2.4.1.4 | dimer |
2 * 72000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 72822, sequence calculation |
-, 736140 |
| 2.4.1.4 | homodimer |
three-dimensional structure and dimer interface analysis. The quaternary organization is likely to participate in the enhanced thermal stability of the protein. Structure comparison with the amylosucrase from Neisseria polysaccharea, overview |
720052 |
| 2.4.1.4 | homotetramer |
4 * 66000, SDS-PAGE |
-, 757054 |
| 2.4.1.4 | monomer |
- |
-, 756235, 756762 |
| 2.4.1.4 | monomer |
1 * 70000, SDS-PAGE |
-, 489141, 757037 |
