EC Number   |
Subunits |
Reference |
|---|
    1.5.3.1 | ? |
x * 43000, calculated, x * 51000, SDS-PAGE |
-, 671547 |
| 1.5.3.1 | ? |
x * 43000, SDS-PAGE |
-, 742952, 765379 |
| 1.5.3.1 | ? |
x * 43000, SDS-PAGE, recombinant protein |
-, 765378 |
| 1.5.3.1 | ? |
x * 51000 |
-, 724775 |
| 1.5.3.1 | dimer |
or trimer, alpha,beta or alpha,beta2, 100000 (alpha), 55000 (beta), SDS-PAGE |
392380 |
| 1.5.3.1 | heterooctamer |
4 * 54000, recombinant alpha-subunnit, + 4 * 43000, recombinant beta-subunit, SDS-PAGE, (alphabeta)4 , the recombinant alpha subunit forms a dimeric structure and behaves as an NADH dehydrogenase, while the beta subunit is a tetramer that has sarcosine oxidase and L-proline dehydrogenase activity.. The SOX complex assembles into the heterooctameric (alphabeta)4 form and shows NADH dehydrogenase activity, transmission electron microscopy and gel filtration |
724937 |
| 1.5.3.1 | heterotetramer |
- |
725317, 742088 |
| 1.5.3.1 | heterotetramer |
1 * 103000 + 1 * 44000 + 1 * 21000 + 1 * 11000, SDS-PAGE |
764037 |
| 1.5.3.1 | heterotetramer |
1 * 110000 + 1 * 44000 + 1 * 21000 + 1 * 10000, calculated from amino acid sequence |
764119 |
| 1.5.3.1 | heterotetramer |
crystallization data |
671702, 675389 |
