PAOX

Polyamine oxidase (exo-N4-amino)
Identifiers
Symbols	PAOX ; PAO
External IDs	OMIM: 615853 MGI: 1916983 HomoloGene: 72096 ChEMBL: 2105 GeneCards: PAOX Gene
EC number	1.5.3.13
Gene ontology Molecular function • receptor binding • polyamine oxidase activity • N(1),N(12)-diacetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity • spermine:oxygen oxidoreductase (spermidine-forming) activity • spermidine:oxygen oxidoreductase (3-aminopropanal-forming) activity • N1-acetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity • N1-acetylspermidine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity Cellular component • peroxisomal matrix Biological process • polyamine metabolic process • polyamine biosynthetic process • polyamine catabolic process • xenobiotic metabolic process • putrescine biosynthetic process • putrescine catabolic process • cellular nitrogen compound metabolic process • small molecule metabolic process • spermidine catabolic process • spermine catabolic process • oxidation-reduction process • positive regulation of spermidine biosynthetic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	196743	212503
Ensembl	ENSG00000148832	ENSMUSG00000025464
UniProt	Q6QHF9	Q8C0L6
RefSeq (mRNA)	NM_152911	NM_153783
RefSeq (protein)	NP_690875	NP_722478
Location (UCSC)	Chr 10: 133.38 – 133.39 Mb	Chr 7: 140.13 – 140.13 Mb
PubMed search

Peroxisomal N(1)-acetyl-spermine/spermidine oxidase is an enzyme that in humans is encoded by the PAOX gene.^[1][2]

References

1. Wu T, Yankovskaya V, McIntire WS (Jun 2003). "Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase". J Biol Chem 278 (23): 20514–25. doi:10.1074/jbc.M302149200. PMID 12660232.
2. "Entrez Gene: PAOX polyamine oxidase (exo-N4-amino)".

Further reading

• Järvinen A, Keinänen TA, Grigorenko NA, et al. (2006). "Guide molecule-driven stereospecific degradation of alpha-methylpolyamines by polyamine oxidase". J. Biol. Chem. 281 (8): 4589–95. doi:10.1074/jbc.M509959200. PMID 16354669.
• 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.
• 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.
• 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.
• 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.
• 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.
• Vujcic S, Liang P, Diegelman P, et al. (2003). "Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion". Biochem. J. 370 (Pt 1): 19–28. doi:10.1042/BJ20021779. PMC 1223169. PMID 12477380.