EC Number   |
Subunits |
Reference |
|---|
   1.2.1.48 | ? |
x * 54000, SDS-PAGE |
390324 |
| 1.2.1.48 | ? |
x * 55496, calculated from the deduced amino acid sequence |
-, 390325 |
| 1.2.1.48 | ? |
x * 57000, SDS-PAGE |
693389 |
| 1.2.1.48 | homodimer |
- |
762634 |
| 1.2.1.48 | homodimer |
2 * 51700, calculated from amino acid sequence |
762884 |
| 1.2.1.48 | homodimer |
2 * 55000, SDS-PAGE |
725656 |
| 1.2.1.48 | homodimer |
human FALDH forms a symmetrical dimer. Each FALDH subunit in the asymmetric unit adopts the canonical aldehyde dehydrogenase fold, including an aminoterminal (N-terminal) cofactor-binding domain (residues 1-79 and 103-208), a catalytic domain (residues 209-419) and an oligomerization domain (residues 82-102 and 420-443) that connects the two subunits of the dimer, and the C-terminal residues 445-460 that form an alpha helix. The recombinant enzyme is truncated and lacks the predicted transmembrane alpha-helical region (residues 464-485) that is not included in the expression constructs, due to incompatibility with the protein production process |
743336 |
| 1.2.1.48 | More |
the dimeric FALDH displays a an element in its C-terminal region, a gatekeeper helix, which extends over the adjacent subunit, controlling the access to the substrate cavity and helping orientate both substrate cavities towards the membrane surface for efficient substrate transit between membranes and catalytic site. Three-dimensional structure analysis and modelling, overview |
743336 |
| 1.2.1.48 | octamer |
8 * 53886, calculated, 8 * 55000, SDS-PAGE |
-, 697840 |
| 1.2.1.48 | octamer |
8 * 55000, determined by SDS-PAGE |
-, 697840 |
