Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. H(+) + L-aspartate = beta-alanine + CO2 Binds 1 pyruvoyl group covalently per subunit. Inhibited by hydroxylamine, phenylhydrazine, sodium borohydride, D-cycloserine, hydrazine, semicarbazine and succinic dehydrazine. L-glutamate, succinate, oxaloacetate, L-serine, L-cysteic acid, beta-hydroxy-DL-aspartate, and D-serine are competitive inhibitors. Optimum pH is about 7.5. The reaction rates at the pH values of 6.8 and 8.0 are about 60% of the pH 7.5 rate. Optimum temperature is 55 degrees Celsius. The half-maximal activity is reached at 26 degrees Celsius and 78 degrees Celsius. Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. Heterooctamer of four alpha and four beta subunits. Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus. Belongs to the PanD family.