Pentaerythritol tetranitrate reductase (PETN reductase)

Pentaerythritol tetranitrate reductase (PETN reductase) is a flavoprotein oxidoreductase enzyme, part of the Old Yellow Enzyme family, that catalyzes the reduction of explosives such as pentaerythritol tetranitrate (PETN), trinitrotoluene (TNT), and picric acid, as well as α,β-unsaturated carbonyl compounds and various nitroaromatics[1][2][3][4][5]. It demonstrates high substrate versatility, including the ability to metabolize steroids, some of which act as substrates and others as inhibitors[1]. PETN reductase operates as a monomeric or dimeric enzyme, requires flavin mononucleotide (FMN) as a cofactor, and uses NADPH as an electron donor[2][4]. It is of particular interest for applications in biocatalysis, bioremediation of environmental pollutants, and green chemistry[5]. PETN reductase is not a therapeutic drug target in the classical sense, but is engineered for industrial and environmental uses such as degrading hazardous nitro-compounds[5][6].

Other names

PETN reductasepentaerythritol tetranitrate reductaseOYE-family reductase

Catalyzes the two-electron reduction of β-unsaturated carbonyl compounds and nitroaromatic/nitroester explosives using NADPH as the electron donor; acts via hydride transfer to electron-deficient substrates through a flavin mononucleotide (FMN) cofactor[1][2][3][4].