Trefzer, ClaudiaRengifo-Gonzalez, MonicaHinner, Marlon J.Schneider, PatriciaMakarov, VadimCole, Stewart T.Johnsson, Kai2010-10-142010-10-142010-10-14201010.1021/ja106357whttps://infoscience.epfl.ch/handle/20.500.14299/55545WOS:000282864100034Benzothiazinones (BTZs) form a new class of potent antimycobacterial agents. Although the target of BTZs has been identified as decaprenylphosphoryl-β-D-ribose 2'-epimerase (DprE1), their detailed mechanism of action remains obscure. Here we demonstrate that BTZs are activated in the bacterium by reduction of an essential nitro group to a nitroso derivative, which then specifically reacts with a cysteine residue in the active site of DprE1.GlutathioneResiduesArabinantext::journal::journal article::research article