EC Number   |
Subunits |
Reference  |
|---|
    3.5.1.54 | dimer |
2 * 68000, His-tagged recombinant enzyme, SDS-PAGE, 2 * 65401, sequence calculation |
-, 667267 |
| 3.5.1.54 | dimer |
2 * 61999, sequence calculation |
-, 668661 |
| 3.5.1.54 | tetramer |
4 * 66223, sequence calculation |
669098 |
| 3.5.1.54 | homohexamer |
6 * 50000, recombinant enzyme, SDS-PAGE |
733034 |
| 3.5.1.54 | ? |
x * 65000, about, recombinant His8-tagged enzyme, SDS-PAGE |
-, 733342 |
| 3.5.1.54 | dimer |
enzyme domain architecture, overview. Both the N- and the C-domains require dimerization for their optimal activities |
734220 |
| 3.5.1.54 | homodimer |
2 * 190000, recombinant enzyme, SDS-PAGE |
-, 744532 |
| 3.5.1.54 | More |
analysis of interactions between the KlUA monomers |
-, 744532 |
| 3.5.1.54 | More |
urea amidolyase is composed of urea carboxylase (UC) and allophanate hydrolase (AH) domains. KlUC and KlAH are monomeric and dimeric in solution, respectively. The relatively smaller UC-AH interface therefore does not play a major role in the UA holo-enzyme assembly. In the isolated KlAH, the active sites are located near the dimer interface. The extensive interactions at the dimer interface most likely stabilize the structure of the active sites. Consistent with this, the G559E/G572E mutation that renders the isolated KlAH monomeric severely inhibited its activity |
-, 744532 |
| 3.5.1.54 | dimer |
N-terminal enzyme amidase domain AtzF467 |
752542 |
