The molecular basis of action of<unk> , and other related drugs clorobiocin and coumermycin A1 has been examined. Aminocoumarins are very potent inhibitors of bacterial DNA gyrase and work by targeting the GyrB subunit of the enzyme involved in energy transduction.<unk>  as well as the other aminocoumarin antibiotics act as competitive inhibitors of the ATPase reaction catalysed by GyrB. The potency of<unk>  is considerably higher than that of the fluoroquinolones that also target DNA gyrase, but at a different site on the enzyme. The GyrA subunit is involved in the DNA nicking and ligation activity.<unk>  has been shown to weakly inhibit the C-terminus of the eukaryotic Hsp90 protein (high micromolar IC50). Modification of the<unk>  scaffold has led to more selective Hsp90 inhibitors.<unk>  has also been shown to bind and activate the Gram-negative lipopolysaccharide transporter LptBFGC. The ATP binding pocket of polymerase theta is blocked by<unk>  resulting in a loss of ATPase activity. This results in the loss of microhomology-mediated end joining as a pathway for homologous recombination deficient cells to circumvent DNA damaging agents. The action of<unk>  is syngeristic with PARP inhibitors for reducing tumor size in a mouse model.
Novobiocin
Domoic acid
Hepatotoxin
Kaliotoxin
Psalmotoxin
Grammotoxin
Transfluthrin
Hemotoxin