ATP-dependent dethiobiotin synthetase (BioD)

ATP-dependent dethiobiotin synthetase, commonly referred to as BioD or DTBS, is an essential enzyme in the biotin (vitamin B7) biosynthesis pathway of various bacteria, fungi, and plants. It catalyzes the ATP-dependent insertion of carbon dioxide into 7,8-diaminononanoate (DAPA) to form the ureido ring of dethiobiotin, which is the penultimate step in the production of biotin. This enzyme is of significant interest as a therapeutic target because the de novo biotin synthesis pathway is essential for the survival and pathogenesis of many microbes, including Mycobacterium tuberculosis, but is entirely absent in humans and other mammals. Consequently, inhibitors of BioD offer a high degree of selectivity, potentially providing a novel class of narrow-spectrum antibiotics with minimal host toxicity. Current research focuses on developing small-molecule inhibitors, such as tetrazole derivatives and substrate analogs, to combat multi-drug resistant infections by disrupting the pathogen's metabolic homeostasis.

Other names

Dethiobiotin synthaseDTBS7,8-diaminononanoate carbamoyltransferase7,8-diaminopelargonic acid carbamoyltransferaseBioDDethiobiotin synthetase

Dethiobiotin synthetase inhibitor