SMOX

SMOX
Identifiers
Aliases	SMOX, C20orf16, PAO, PAO-1, PAO1, PAOH, PAOH1, SMO, spermine oxidase
External IDs	OMIM: 615854; MGI: 2445356; HomoloGene: 69268; GeneCards: SMOX; OMA:SMOX - orthologs
EC number	1.5.3.16
Gene location (Human)
Chr.	Chromosome 20 (human)
End	4,187,747 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	131,525,922 bp
RNA expression pattern
	Top expressed in
	amygdala; ; C1 segment; ; putamen; ; substantia nigra; ; hypothalamus; ; nucleus accumbens; ; monocyte; ; cartilage tissue; ; caudate nucleus; ; Region I of hippocampus proper;
	Top expressed in
	triceps brachii muscle; ; sternocleidomastoid muscle; ; vastus lateralis muscle; ; knee joint; ; gastrocnemius muscle; ; granulocyte; ; medial head of gastrocnemius muscle; ; skeletal muscle tissue; ; fetal liver hematopoietic progenitor cell; ; molar;
	More reference expression data
	; ;
	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; nucleus; cytoplasm; nucleoplasm; nuclear membrane; intracellular membrane-bounded organelle;
Biological process	polyamine catabolic process; spermine catabolic process; polyamine biosynthetic process;
	Sources:Amigo / QuickGO
Orthologs
	54498
	228608
	ENSG00000088826
	ENSMUSG00000027333
	Q9NWM0
	Q99K82
NM_001270691; NM_175839; NM_175840; NM_175841; NM_175842;
	NM_019025
NM_001177833; NM_001177834; NM_001177835; NM_001177836; NM_001177837;
	NM_001177838; NM_001177839; NM_001177840; NM_145533
	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
	Wikidata
View/Edit Human	View/Edit Mouse

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

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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000088826 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000027333 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ 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.
^ ^a ^b "Entrez Gene: SMOX spermine oxidase".

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.

This article on a gene on human chromosome 20 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000088826 – Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid11454677-5] 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.

[pmid12398765-6] 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.

[entrez-7] "Entrez Gene: SMOX spermine oxidase".

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[6]

[7]

SMOX

Function

References

Further reading