Reactome | SMOX-3 oxidises SPN to SPM

SMOX-3 oxidises SPN to SPM

Stable Identifier

R-HSA-141341

Type

Reaction [transition]

Species

Homo sapiens

Compartment

peroxisomal matrix, cytosol

ReviewStatus

5/5

Locations in the PathwayBrowser

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Metabolism (Homo sapiens)

- Biological oxidations (Homo sapiens)
  - Phase I - Functionalization of compounds (Homo sapiens)
    - Amine Oxidase reactions (Homo sapiens)
      - PAOs oxidise polyamines to amines (Homo sapiens)
        
        SMOX-3 oxidises SPN to SPM (Homo sapiens)
- Metabolism of amino acids and derivatives (Homo sapiens)
  - Metabolism of polyamines (Homo sapiens)
    - Interconversion of polyamines (Homo sapiens)
      - SMOX-3 oxidises SPN to SPM (Homo sapiens)

General

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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