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Spermine oxidase (SMOX) is a flavoprotein enzyme that plays a central role in polyamine catabolism. It catalyzes the direct oxidation of spermine to spermidine, producing hydrogen peroxide (H₂O₂) and 3-aminopropanal as byproducts. This reaction is FAD-dependent. SMOX regulates intracellular concentrations of spermine and spermidine, which are essential for cell growth, differentiation, and survival. By producing H₂O₂ as a byproduct, SMOX contributes to cellular oxidative stress responses. Altered SMOX activity has been implicated in various diseases, including cancer progression and liver function abnormalities.
Catalyzes the oxidation of spermine to spermidine, producing hydrogen peroxide and 3-aminopropanal.
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