SMOX-3 oxidises SPN to SPM

Stable Identifier
R-HSA-141341
Type
Reaction
Species
Homo sapiens
Compartment
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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).

Literature References
PubMed ID Title Journal Year
12727196 Properties of purified recombinant human polyamine oxidase, PAOh1/SMO

Frydman, B, Casero RA, Jr, Devereux, W, Wang, Y, Woster, PM, Murray-Stewart, T, Hacker, A

Biochem Biophys Res Commun 2003
12141946 Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin

Diegelman, P, Bacchi, CJ, Vujcic, S, Kramer, DL, Porter, CW

Biochem J 2002
Participants
Participates
Catalyst Activity

spermine:oxygen oxidoreductase (spermidine-forming) activity of SMOX-3 [cytosol]

Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created
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