EC Number   |
Subunits |
Reference |
|---|
    1.2.1.47 | ? |
x * 55000, SDS-PAGE |
-, 288255 |
| 1.2.1.47 | homotrimer |
3 * 52000, SDS-PAGE |
-, 726537 |
| 1.2.1.47 | More |
conformation of the inter-domain linker in the P1 ALDH9A1-NAD+ structure, modeling, overview. The in-solution quaternary structure of ALDH9A1 is determined using SAXS |
762675 |
| 1.2.1.47 | More |
each ALDH monomer displays a typical ALDHs fold composed of an oligomerization domain (residues 128-145 and 479-494), a coenzyme domain (residues 1-127, 146-257, 470-478), a catalytic domain (residues 258-448) with the catalytic Cys288, and an interdomain linker highly conserved in amino-acid sequence and folding. Nonetheless, structural comparison reveals a position and a unique fold of the interdomain linker of ALDH9A1. The oligomerization domain wraps over the groove between the catalytic and coenzyme domains of the other monomer forming the dimer |
762831 |
| 1.2.1.47 | tetramer |
4 * 56000, dimer-of-dimers, recombinant His-tagged enzyme, SDS-PAGE |
762831 |
| 1.2.1.47 | tetramer |
enzyme ALDH9A1 forms the classic ALDH superfamily dimer-of-dimers tetramer in solution. Analytical ultracentrifugation, small-angle X-ray scattering (SAXS), and negative stain electron microscopy are used for analysis |
762675 |
| 1.2.1.47 | trimer |
3 * 55000, SDS-PAGE |
-, 288254, 691376 |
