SMOX

Spermine oxidase is an enzyme that in humans is encoded by the SMOX gene.[5][6][7]

SMOX
Identifiers
Aliases	SMOX, C20orf16, PAO, PAO-1, PAO1, PAOH, PAOH1, SMO, spermine oxidase
External IDs	OMIM: 615854 MGI: 2445356 HomoloGene: 69268 GeneCards: SMOX
EC number	1.5.3.16
Gene location (Human) Chr. Chromosome 20 (human)[1] Band 20p13 Start 4,120,980 bp[1] End 4,187,747 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2|2 F1 Start 131,491,496 bp[2] End 131,525,922 bp[2]
RNA expression pattern More reference expression data
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 • cell nucleus • cytoplasm • nucleoplasm • not the membrane • intracellular membrane-bounded organelle Biological process • polyamine catabolic process • spermine catabolic process • polyamine biosynthetic process • oxidation-reduction process Sources:Amigo / QuickGO
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 NP_787033 NP_787034 NP_787035 NP_787036	NP_001171304 NP_001171305 NP_001171306 NP_001171307 NP_001171308 NP_001171309 NP_001171310 NP_001171311 NP_663508
Location (UCSC)	Chr 20: 4.12 – 4.19 Mb	Chr 2: 131.49 – 131.53 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000088826 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000027333 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Wang Y, Devereux W, Woster PM, Stewart TM, Hacker A, Casero RA (July 2001). "Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure". Cancer Research. 61 (14): 5370–3. PMID 11454677.
6. Murray-Stewart T, Wang Y, Devereux W, Casero RA (December 2002). "Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics". The Biochemical Journal. 368 (Pt 3): 673–7. doi:10.1042/BJ20021587. PMC 1223052. PMID 12398765.
7. "Entrez Gene: SMOX spermine oxidase".

Further reading

• Seiler N (June 2004). "Catabolism of polyamines". Amino Acids. 26 (3): 217–33. doi:10.1007/s00726-004-0070-z. PMID 15221502. S2CID 22119330.
• Hölttä E (January 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, Hibasami H, Nakashima K (1988). "Purification by affinity chromatography and characterization of porcine liver cytoplasmic polyamine oxidase". The International Journal of Biochemistry. 20 (7): 695–702. doi:10.1016/0020-711X(88)90164-4. PMID 3181599.
• Vujcic S, Diegelman P, Bacchi CJ, Kramer DL, Porter CW (November 2002). "Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin". The Biochemical Journal. 367 (Pt 3): 665–75. doi:10.1042/BJ20020720. PMC 1222929. PMID 12141946.
• Cervelli M, Polticelli F, Federico R, Mariottini P (February 2003). "Heterologous expression and characterization of mouse spermine oxidase". The Journal of Biological Chemistry. 278 (7): 5271–6. doi:10.1074/jbc.M207888200. PMID 12458219.
• Wang Y, Murray-Stewart T, Devereux W, Hacker A, Frydman B, Woster PM, Casero RA (May 2003). "Properties of purified recombinant human polyamine oxidase, PAOh1/SMO". Biochemical and Biophysical Research Communications. 304 (4): 605–11. doi:10.1016/S0006-291X(03)00636-3. PMID 12727196.
• Cervelli M, Bellini A, Bianchi M, Marcocci L, Nocera S, Polticelli F, Federico R, Amendola R, Mariottini P (February 2004). "Mouse spermine oxidase gene splice variants. Nuclear subcellular localization of a novel active isoform". European Journal of Biochemistry. 271 (4): 760–70. doi:10.1111/j.1432-1033.2004.03979.x. PMID 14764092.
• Pledgie A, Huang Y, Hacker A, Zhang Z, Woster PM, Davidson NE, Casero RA (December 2005). "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". The Journal of Biological Chemistry. 280 (48): 39843–51. doi:10.1074/jbc.M508177200. PMID 16207710.