EC Number   |
Subunits |
Reference |
|---|
    1.8.1.2 | ? |
x * 60000, determined by SDS-PAGE |
696893 |
| 1.8.1.2 | dimer |
1 * 75000 plus 1 * 41000, SDS-PAGE |
-, 743706 |
| 1.8.1.2 | dodecamer |
- |
765285 |
| 1.8.1.2 | dodecamer |
alpha8,beta4, 8 * 58000-60000 + 4 * 54000-57000, sedimentation under denaturing conditions |
287801, 392952, 392962 |
| 1.8.1.2 | dodecamer |
NADPH-dependent assimilatory sulfite reductase (SiR) is composed of two subunits. One is a multidomain flavin binding reductase (SiRFP) and the other an iron-containing oxidase (SiRHP). Tight binding between SiRFP and SiRHP is incompatible with the electron transfer-competent interface, suggesting that the dodecameric holoenzyme consists of four SiRFP/SiRHP heterodimers and four free SiRFP molecules. Six electrons come two at a time from three NADPH cofactors to complete catalysis, which means that SiRHP must interact with SiRFP three times for every SO3(2-) that binds |
764151 |
| 1.8.1.2 | dodecamer |
SDS-PAGE |
392962, 392976 |
| 1.8.1.2 | dodecamer |
the dodecameric complex of flavoprotein reductase subunits (SiRFP) and hemoprotein oxidase subunits (SiRHP). Small-angle neutron scattering solution structures of the interaction of SiRFP show, how both SiRHP binding to, and reduction of, SiRFP positions SiRFP for electron transfer between the subunits |
765286 |
| 1.8.1.2 | heterodimer |
- |
-, 764536 |
| 1.8.1.2 | heterotetramer |
two alpha- and two beta-subunits, encoded by the MET10 and MET5 gene, respectively |
698012 |
| 1.8.1.2 | hexamer |
alpha2,beta2,gamma2, 2 * 50000 + 2 * 42000 + 2 * 12500, SDS-PAGE |
392979 |
