4.1.1.11	additional information	the Escherichia coli aspartate decarboxylase, ADC, is hexameric	-, 748086	
4.1.1.11	octamer	two tetramers forming a pseudo fourfold rotational symmetry, the enzyme protein shows a double-psi beta-barrel structure	682753	
4.1.1.11	?	x * 13800, SDS-PAGE	682386	
4.1.1.11	?	x * 14100, pi-protein, calculated from the amino acid sequence	649350	
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	
4.1.1.11	?	x * 58000, SDS-PAGE	665041