Enoyl–acyl carrier protein reductase (ENR)

Enoyl–acyl carrier protein reductase is a key enzyme of the bacterial type II fatty acid synthesis pathway, catalyzing the final reduction step in each elongation cycle where an enoyl-ACP substrate is reduced to a saturated acyl-ACP, enabling cellular fatty acid production[1][2][5][7]. ENR is highly conserved and essential in bacteria but structurally distinct from mammalian enzymes, making it an attractive target for new antibiotics with minimal off-target effects[5][2]. Several structural homologs exist across pathogens, with forms such as FabI, FabK, FabL, and FabV. These enzymes are inhibited by molecules such as triclosan and have been studied in the context of antimicrobial drug development[5][6][1][3]. ENR enzymes either utilize NADH or NADPH as a reductant, sometimes with a flavin mononucleotide (FMN) cofactor, depending on species[2][1]. Inhibitor binding typically blocks fatty acid synthesis, leading to bacteriostatic or bactericidal effects[5][1][6].

Other names

Enoyl-[acyl-carrier-protein] reductaseFabIFabKENR

Competitive inhibition (e.g. Triclosan binds competitively with NADH, blocking catalytic activity); Direct binding to active site and stabilization of inactive enzyme-inhibitor complex; Other inhibitors may act via non-competitive mechanisms by binding to different enzyme conformations.