Spermine oxidase (SMOX, PAOh1, SMO) is a polyamine oxidase flavoenzyme that catalyses the oxidation of spermine (SPN) to spermidine (SPM). It plays an important role in the regulation of endogenous polyamine intracellular concentration. Five different isozymes are produced by alternative splicing with isozyme 3 being the major isoform and possessing the highest affinity for spermine. It is highly inducible by specific antitumor polyamine analogues (Wang et al. 2001).
Frydman, B, Casero RA, Jr, Devereux, W, Wang, Y, Woster, PM, Murray-Stewart, T, Hacker, A
Diegelman, P, Bacchi, CJ, Vujcic, S, Kramer, DL, Porter, CW
spermine:oxygen oxidoreductase (spermidine-forming) activity of SMOX-3 [cytosol]
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