Tyramine oxidase (tynA) (tynA)

Tyramine oxidase (TynA) is a copper-containing enzyme primarily characterized in bacteria such as Escherichia coli, where it facilitates the oxidative deamination of primary amines like tyramine and phenylethylamine [UniProt P0AEC8, PMID: 1353444]. This enzymatic reaction produces the corresponding aldehyde, ammonia, and hydrogen peroxide, enabling the bacterium to utilize amines as a nitrogen source [PMID: 9461325]. TynA belongs to the family of copper-containing amine oxidases (CuAOs) and utilizes a unique, protein-derived cofactor known as topaquinone (TPQ), which is formed by the post-translational modification of a specific tyrosine residue [PMID: 10521336]. While TynA itself is not a common target for human clinical therapeutics, it is extensively studied as a structural and functional model for human CuAOs, including vascular adhesion protein-1 (VAP-1/AOC3) and diamine oxidase (DAO/AOC1) [PMID: 11932214]. Inhibitors of TynA, such as various hydrazine derivatives and semicarbazide, are used in research to explore the mechanisms of amine oxidation and to develop selective inhibitors that could potentially target related enzymes involved in human inflammatory and metabolic diseases [ChEMBL CHEMBL2595, PMID: 1353444].

Other names

Copper-containing amine oxidasePhenylethylamine oxidaseCuAOPrimary-amine:oxygen oxidoreductase (deaminating) (copper-containing)Bacterial monoamine oxidase

Covalent inhibition of the topaquinone (TPQ) cofactor