SMOX-3 oxidises SPN to SPM

Stable Identifier
R-HSA-141341
Type
Reaction [transition]
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
12141946 Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin

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

Biochem J 2002
12727196 Properties of purified recombinant human polyamine oxidase, PAOh1/SMO

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

Biochem Biophys Res Commun 2003
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
spermine:oxygen oxidoreductase (spermidine-forming) activity of SMOX-3 [cytosol]
Physical Entity
Activity
Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created