SMOX

SMOX
Identifiers
Aliases	SMOX, C20orf16, PAO, PAO-1, PAO1, PAOH, PAOH1, SMO, spermine oxidase
External IDs	MGI: 2445356 HomoloGene: 69268 GeneCards: SMOX
EC number	1.5.3.16
Gene ontology Molecular function • N1-acetylspermine:oxygen oxidoreductase (N1-acetylspermidine-forming) activity • polyamine oxidase activity • oxidoreductase activity • norspermine:oxygen oxidoreductase activity • spermine:oxygen oxidoreductase (spermidine-forming) activity Cellular component • cytosol • nucleus • cytoplasm Biological process • polyamine catabolic process • spermine catabolic process • polyamine biosynthetic process • oxidation-reduction process Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	54498	228608
Ensembl	ENSG00000088826	ENSMUSG00000027333
UniProt	Q9NWM0	Q99K82
RefSeq (mRNA)	NM_001270691 NM_175839 NM_175840 NM_175841 NM_175842	NM_001177833 NM_001177834 NM_001177835 NM_001177836 NM_001177837 NM_001177838 NM_001177839 NM_001177840 NM_145533
RefSeq (protein)	NP_001257620.1 NP_787033.1 NP_787034.1 NP_787035.1 NP_787036.1	NP_001171304.1 NP_001171305.1 NP_001171306.1 NP_001171307.1 NP_001171309.1 NP_001171310.1 NP_001171311.1 NP_663508.1
Location (UCSC)	Chr 20: 4.12 – 4.19 Mb	Chr 2: 131.49 – 131.53 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

Spermine oxidase is an enzyme that in humans is encoded by the SMOX gene.^[3][4][5]

The product of this gene is the polyamine oxidase. This enzyme potentially represents a new class of catabolic enzymes in the mammalian polyamine metabolic pathway capable of the efficient oxidation of polyamines. More than five transcript variants encoding four active isoenzymes have been identified for this gene, however, not all variants have been fully described. The characterized isoenzymes have distinctive biochemical characteristics and substrate specificities, suggesting the existence of additional levels of complexity in polyamine catabolism.^[5]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Wang Y; Devereux W; Woster PM; Stewart TM; Hacker A; Casero RA Jr (Jul 2001). "Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure". Cancer Res. 61 (14): 5370–3. PMID 11454677.
4. Murray-Stewart T, Wang Y, Devereux W, Casero RA Jr (Dec 2002). "Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics". Biochem J. 368 (Pt 3): 673–7. doi:10.1042/BJ20021587. PMC 1223052. PMID 12398765.
5. "Entrez Gene: SMOX spermine oxidase".

Further reading

• Seiler N (2005). "Catabolism of polyamines". Amino Acids. 26 (3): 217–33. doi:10.1007/s00726-004-0070-z. PMID 15221502.
• Hölttä E (1977). "Oxidation of spermidine and spermine in rat liver: purification and properties of polyamine oxidase". Biochemistry. 16 (1): 91–100. doi:10.1021/bi00620a015. PMID 12798.
• Tsukada T, Furusako S, Maekawa S, et al. (1988). "Purification by affinity chromatography and characterization of porcine liver cytoplasmic polyamine oxidase". Int. J. Biochem. 20 (7): 695–702. doi:10.1016/0020-711X(88)90164-4. PMID 3181599.
• Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
• Vujcic S, Diegelman P, Bacchi CJ, et al. (2002). "Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin". Biochem. J. 367 (Pt 3): 665–75. doi:10.1042/BJ20020720. PMC 1222929. PMID 12141946.
• Cervelli M; Polticelli F; Federico R; Mariottini P (2003). "Heterologous expression and characterization of mouse spermine oxidase". J. Biol. Chem. 278 (7): 5271–6. doi:10.1074/jbc.M207888200. PMID 12458219.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Wang Y, Murray-Stewart T, Devereux W, et al. (2003). "Properties of purified recombinant human polyamine oxidase, PAOh1/SMO". Biochem. Biophys. Res. Commun. 304 (4): 605–11. doi:10.1016/S0006-291X(03)00636-3. PMID 12727196.
• Clark HF, Gurney AL, Abaya E, et al. (2003). "The Secreted Protein Discovery Initiative (SPDI), a Large-Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins: A Bioinformatics Assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Cervelli M, Bellini A, Bianchi M, et al. (2004). "Mouse spermine oxidase gene splice variants. Nuclear subcellular localization of a novel active isoform". Eur. J. Biochem. 271 (4): 760–70. doi:10.1111/j.1432-1033.2004.03979.x. PMID 14764092.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Pledgie A, Huang Y, Hacker A, et al. (2006). "Spermine oxidase SMO(PAOh1), Not N1-acetylpolyamine oxidase PAO, is the primary source of cytotoxic H2O2 in polyamine analogue-treated human breast cancer cell lines". J. Biol. Chem. 280 (48): 39843–51. doi:10.1074/jbc.M508177200. PMID 16207710.