4.1.1.20	metabolism	binding of PLP initiates rearrangements within the active site, specifically the reorientation of Arg169, His218, and His22, which is propagated to the active-site loop, through Arg169. The substrate, meso-diaminopimelate, is positioned through interactions with conserved active-site residues to form an additional hydrogen bond to His220. This stabilizes the closed active-site loop conformation, mediated through Arg169, and can only occur when the D-stereocenter is oriented for decarboxylation	772815	
4.1.1.20	metabolism	diaminopimelate decarboxylase (DAPDC) catalyzes the conversion of meso-2,6-diaminopimelate to lysine and carbon dioxide in the final step of the diaminopimelate (DAP) pathway	-, 747204	
4.1.1.20	metabolism	enzyme meso-diaminopimelic acid decarboxylase (DAPDC) catalyzes the final step in the de novo L-lysine biosynthetic pathway by converting meso-diaminopimelic acid (meso-DAP) into L-lysine by decarboxylation reaction	-, 747000	
4.1.1.20	metabolism	the enzyme catalyzes the irreversible and stereospecific decarboxylation of meso-diaminopimelate (meso-DAP) in the final step of the diaminopimelate (DAP) biosynthesis pathway	-, 748217	
4.1.1.20	additional information	dimerization of bacterial diaminopimelate decarboxylase is essential for catalysis	-, 748217	
4.1.1.20	physiological function	expression of DAPDC1 rescues Escherichia coli that harbors a mutation in the gene encoding DAPDC. DAPDC1 is only able to rescue the mutant when its expression is repressed by glucose	772815	
4.1.1.20	physiological function	expression of DAPDC2 rescues Escherichia coli that harbors a mutation in the gene encoding DAPDC. DAPDC2 is only able to rescue the mutant when its expression is repressed by glucose	772815	
4.1.1.20	physiological function	the product of the reaction, L-lysine, is an important building block for the biosynthesis of the peptidoglycan cell wall, housekeeping proteins, and virulence factors of bacteria	-, 748217