3.5.1.54	?	x * 65000, about, recombinant His8-tagged enzyme, SDS-PAGE	-, 733342	
3.5.1.54	dimer	2 * 61999, sequence calculation	-, 668661	
3.5.1.54	dimer	2 * 68000, His-tagged recombinant enzyme, SDS-PAGE, 2 * 65401, sequence calculation	-, 667267	
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	dimer	N-terminal enzyme amidase domain AtzF467	752542	
3.5.1.54	homodimer	2 * 190000, recombinant enzyme, SDS-PAGE	-, 744532	
3.5.1.54	homohexamer	6 * 50000, recombinant enzyme, SDS-PAGE	733034	
3.5.1.54	additional information	analysis of interactions between the KlUA monomers	-, 744532	
3.5.1.54	additional information	structure analysis of the amidase domain of AtzF, the allophanate hydrolase from the cyanuric acid-mineralizing multienzyme complex, overview. AtzF forms a large, ca. 660-kDa, multienzyme complex with cyanuric acid amidohydrolase AtzD and biuret amidohydrolase AtzE. Analysis of the multimerization of AtzF and Atzf467 by small-angle x-ray scattering (SAXS)	752542	
3.5.1.54	additional information	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	tetramer	4 * 66223, sequence calculation	669098