EC Number   |
Subunits  |
Reference |
|---|
    4.1.1.11 | tetramer |
4 * 14000 |
650836 |
| 4.1.1.11 | tetramer |
4 * 16000, recombinant enzyme, inactive pi-proenzyme, which is cleaved into the 13.22 kDa alpha-subunit and 2.74 kDa beta-subunit, processing is not essential for tetramer formation, SDS-PAGE |
-, 653749 |
| 4.1.1.11 | tetramer |
active enzyme is a tetramer composed of three alpha- and beta-subunits and an incompletely processed pi-protein |
-, 649350 |
| 4.1.1.11 | tetramer |
crystallographic data. Tetramer with pseudofour-fold rotational symmetry. The subunits are six-stranded beta-barrels capped by small alpha-helices at each end. The active sites are located between adjacent subunits |
3949 |
| 4.1.1.11 | tetramer |
the bacterial ADC is a tetramer containing approximately 120 amino acids in each subunit |
-, 749207 |
| 4.1.1.11 | tetramer |
x * 2800, beta, + x * 11000, alpha, + x * 13800, pi, SDS-PAGE, enzyme comprises principally the unprocessed pi-subunit, with a small proportion of the alpha-subunit and the beta-subunit. The enzyme is synthesized initially as an inactive proenzyme, the pi-protein, which is proteolytically cleaved at a specific X-Ser bond to produce a beta-subunit with XOH at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus, derived from serine |
3950 |
