Fatty acid synthase enoyl-acyl carrier protein reductase (ER (in the context of fatty acid synthase), ENR (more generally), or FabI (in prokaryotes))

Fatty acid synthase enoyl-acyl carrier protein reductase is an essential enzymatic domain or subunit within the fatty acid synthase (FAS) system. In eukaryotes (type I FAS), it is one of several catalytic domains of a multi-functional polypeptide responsible for reducing enoyl-ACP intermediates to saturated acyl-ACP, using NADPH as an electron donor[2][1]. In bacteria (type II FAS), the enzyme is a stand-alone protein (often called ENR or FabI) and is targeted by several narrow-spectrum antibiotics due to its crucial role in cell membrane biosynthesis[4][5]. Human FAS activity is normally low in most tissues but is highly upregulated in cancers and certain metabolic disorders, making this enzyme a target of interest in oncology and metabolic disease research[2]. The bacterial enzyme has structural and mechanistic differences from the mammalian counterpart, enabling selective drug targeting[3][4][5]. ENR/FabI is widely studied as a point of inhibition for both antibacterial and anticancer agents.

Other names

Enoyl-acyl carrier protein reductaseEnoyl-ACP reductaseENRFabIEnoyl-[acyl-carrier-protein] reductase

Competitive and uncompetitive inhibition with respect to substrate or cofactor binding (triclosan competes with NADH on the ENR active site); Inhibition leads to disruption of bacterial fatty acid synthesis, causing bacteriostatic or bactericidal effects