EC Number |
Subunits |
Reference |
---|
1.5.1.2 | ? |
x * 28140, calculated from SDS-PAGE |
-, 726110 |
1.5.1.2 | decamer |
- |
675361, 676969 |
1.5.1.2 | decamer |
10 * 28112, calculation from nucleotide sequence, SDS-PAGE |
392116 |
1.5.1.2 | decamer |
10*32000-35600, estimated by SDS-PAGE, confirmed by spectrometric analysis |
676952 |
1.5.1.2 | decamer |
five homodimer subunits |
675382 |
1.5.1.2 | dimer |
- |
675361 |
1.5.1.2 | dodecamer |
12 * 28000, SDS-PAGE |
741069 |
1.5.1.2 | More |
enzyme forms a concentration-dependent decamer in solution, sedimentation velocity data |
740763 |
1.5.1.2 | More |
enzyme is a decamer of five dimers, crystallization data |
740491 |
1.5.1.2 | multimer |
x * 30000, SDS-PAGE. Enzyme self-associates to form large multimeric complexes. The most stable multimeric configuration is a decamer, which can further self-associate to form higher order complexes |
-, 701063 |