Bacterial azoreductase

Bacterial azoreductase is a class of flavin mononucleotide (FMN)-dependent oxidoreductase enzymes found widely in bacteria. These enzymes catalyze the reductive cleavage of azo bonds (−N=N−), using NADH or NADPH as electron donors, to degrade azo dyes and activate or deactivate azo prodrugs. Structurally, azoreductases such as AzoR and AzoA have a flavodoxin-like fold and assemble as homodimers, each with an FMN binding site[1][2][3]. Azoreductases are important in the bioremediation of industrial dyes, metabolism of certain food additives, and activation or deactivation of pharmaceuticals with azo linkages (such as sulfasalazine), particularly in the gut microbiome[5]. The substrate specificity of bacterial azoreductases varies, but they generally show broad activity against a range of azo compounds[3]. These enzymes can be exploited in biotechnological applications, such as wastewater treatment and prodrug design, but also pose safety concerns due to the possible production of toxic aromatic amines as byproducts of azo bond reduction.

Other names

Azoreductaseazo reductaseNAD(P)H-dependent azoreductaseFMN-azoreductaseAzoAAzoRBVU5

Catalyzes the reductive cleavage of azo (-N=N-) bonds in dyes and prodrugs, using NAD(P)H as the electron donor to produce colorless aromatic amines[1][2][3][5].