Diaminopimelate dehydrogenase (DAPDH)

Diaminopimelate dehydrogenase (DAPDH) is an NADP+-dependent oxidoreductase enzyme that catalyzes the reversible oxidative deamination of meso-2,6-diaminopimelate to L-2-amino-6-oxopimelate and ammonia, playing a critical role in the bacterial lysine biosynthetic pathway. This pathway is absent in mammals, making DAPDH a promising target for antibiotics and herbicides. The enzyme has been studied structurally and functionally; it is specific for its native substrate in most organisms, though some variants display broader substrate specificity and are valuable as biocatalysts for D-amino acid synthesis. DAPDH is not used as a therapeutic target in humans, but is of great interest for antimicrobial drug development and industrial biotechnology.

Other names

meso-diaminopimelate dehydrogenasemeso-DAPDHmeso-2,6-diaminopimelate dehydrogenasemeso-alpha,epsilon-diaminopimelate dehydrogenaseEC 1.4.1.16

Inhibitors would block the lysine biosynthetic pathway, thereby inhibiting bacterial growth Enzyme used as a biocatalyst for the asymmetric synthesis of D-amino acids