EC Number   |
Subunits |
Reference |
|---|
    1.1.1.215 | dimer |
2 * 35000, SDS-PAGE |
-, 286278 |
| 1.1.1.215 | dimer |
2 * 36000, SDS-PAGE |
286279 |
| 1.1.1.215 | hexamer |
6 * 33200, SDS-PAGE |
-, 721369 |
| 1.1.1.215 | More |
enzyme consists of a gamma subunit, a flavoprotein subunit, and a cytochrome c subunit with molecular masses of about 27, 65, and 47 kDa, respectively |
-, 760370 |
| 1.1.1.215 | More |
the enzyme shows a structure consisting of two-compact domains separated by a deep active cleft. This typical topology is conserved in other 2-HDH. The smaller domain is the substrate binding domain or catalytic domain, which is formed from N-terminal residues 2-102 and C-terminal residues 288-317. It is folded into a five-stranded parallel beta-sheet flanked by five alpha-helices, forming a modified Rossmann topology. The larger domain is responsible for binding the cofactor and contains a conserved [GXGXXG (X17) D] motif that is characteristic of the NAD(P)H/NAD(P)+-binding region. It consists of residues 103-287, forming a seven-stranded parallel beta-sheet flanked by seven alpha-helices. A two-stranded hinge connects the two domains showing flexibility during catalysis |
-, 742168 |
| 1.1.1.215 | octamer |
8 * 15000, SDS-PAGE |
286273 |
| 1.1.1.215 | trimer |
- |
286275 |
| 1.1.1.215 | trimer |
1 * 23000 + 1 * 44000 + 1 * 65000, SDS-PAGE |
-, 684567 |
| 1.1.1.215 | trimer |
2 * 43000 + 1 * 34000, SDS-PAGE |
286275 |
| 1.1.1.215 | trimer |
3 * 40000, SDS-PAGE |
286274 |
