Bacterial monoamine oxidase (MAO)

Bacterial monoamine oxidases (MAOs) are FAD-dependent oxidative enzymes that catalyze the breakdown of primary and secondary amines and polyamines. While mammalian MAOs are central regulators of neurotransmitters, bacterial homologs (e.g., from *Thermoanaerobacterales* and *Corynebacterium ammoniagenes*) display broad substrate specificity and extreme thermostability, making them attractive tools in synthetic organic chemistry and biosensing[1][2]. The active site features a canonical "aromatic cage", and the high-resolution structures reveal similarities and some differences compared to human MAOs (such as the absence of C-terminal membrane anchoring domains in some bacterial forms)[1][6]. The physiological role of bacterial MAOs is still being investigated; proposed functions include nitrogen scavenging and polyamine degradation[2]. Nitroreductases, while grouped here in the query, comprise a distinct class of FAD-dependent enzymes involved in the reduction of nitro groups; they are functionally unrelated to MAOs and may play roles in antibiotic resistance, drug metabolism, and detoxification, but specific bacterial data is not detailed in the provided sources. *Note:* For future structured work, it is best to handle "Bacterial monoamine oxidase" and "Bacterial nitroreductase" as **separate targets**, as current results do not support conflation without loss of specificity or scientific rigor[1][2][3][6].

Other names

Monoamine oxidase (general, non-specific to species)Bacterial MAOFlavin amine oxidase (superfamily membership)caMAO (for Corynebacterium ammoniagenes)Thermoanaerobacterales MAO (MAO~Tb~ )

Oxidation of monoamines and polyamines to corresponding aldehydes, with reduction of oxygen to hydrogen peroxide via FAD cofactor. Nitroreductase: cytosolic reduction of nitro groups on substrates (not detailed for bacterial forms here).