7,8-diaminopelargonic acid synthase (DAPA synthase)

7,8-Diaminopelargonic acid synthase (DAPA synthase; EC 2.6.1.62/2.6.1.105), commonly referred to as 7,8-diaminononanoate synthase in functional nomenclature, is a pyridoxal phosphate-dependent aminotransferase that catalyzes the transfer of an amino group from S-adenosyl-L-methionine (SAM) or L-lysine to 7-keto-8-aminopelargonic acid (KAPA), producing 7,8-diaminononanoate (DAPA) in the third-to-last step of de novo biotin biosynthesis. This process is essential for microbial viability and is absent in animals, making the enzyme a valuable antimicrobial drug target. DAPA synthase is encoded by the bioA (or occasionally bioK) gene in various bacteria and is part of a tightly regulated biotin operon cluster

Other names

7,8-diaminononanoate synthase7,8-diaminopelargonic acid synthaseDAPA synthaseDAPA aminotransferase7,8-diaminononanoate transaminasebioA gene product (EC 2.6.1.62, EC 2.6.1.105)

Enzyme inhibitors would typically act by blocking the aminotransferase activity, ultimately depleting biotin synthesis in susceptible bacteria or fungi