L-aspartate alpha-decarboxylase could catalyze the decarboxylation of L-aspartic acid to generate beta-alanine, which is one of key enzymes in pantothenate metabolism, playing an important role in energy and lipid metabolism of all lives. It belongs to a small class of pyruvoyl-dependent enzymes, which has characteristic mechanisms of self-cleavage on pro-enzyme and substrate inactivation during catalysis. Here, we reviewed advances and achievements in molecular mechanism and modification of bacterial L-aspartate alpha-decarboxylase, and expected its application in biosynthesis of beta-alanine.