Spermine oxidase

Details

Name
Spermine oxidase
Synonyms
  • 1.5.3.16
  • C20orf16
  • PAO-1
  • PAOh1
  • Polyamine oxidase 1
  • SMO
Gene Name
SMOX
Organism
Humans
Amino acid sequence
>lcl|BSEQ0001130|Spermine oxidase
MQSCESSGDSADDPLSRGLRRRGQPRVVVIGAGLAGLAAAKALLEQGFTDVTVLEASSHI
GGRVQSVKLGHATFELGATWIHGSHGNPIYHLAEANGLLEETTDGERSVGRISLYSKNGV
ACYLTNHGRRIPKDVVEEFSDLYNEVYNLTQEFFRHDKPVNAESQNSVGVFTREEVRNRI
RNDPDDPEATKRLKLAMIQQYLKVESCESSSHSMDEVSLSAFGEWTEIPGAHHIIPSGFM
RVVELLAEGIPAHVIQLGKPVRCIHWDQASARPRGPEIEPRGEGDHNHDTGEGGQGGEEP
RGGRWDEDEQWSVVVECEDCELIPADHVIVTVSLGVLKRQYTSFFRPGLPTEKVAAIHRL
GIGTTDKIFLEFEEPFWGPECNSLQFVWEDEAESHTLTYPPELWYRKICGFDVLYPPERY
GHVLSGWICGEEALVMEKCDDEAVAEICTEMLRQFTGNPNIPKPRRILRSAWGSNPYFRG
SYSYTQVGSSGADVEKLAKPLPYTESSKTAPMQVLFSGEATHRKYYSTTHGALLSGQREA
ARLIEMYRDLFQQGT
Number of residues
555
Molecular Weight
61818.76
Theoretical pI
5.15
GO Classification
Functions
N1-acetylspermine / norspermine / polyamine oxidase activity / spermine
Processes
cellular nitrogen compound metabolic process / oxidation-reduction process / polyamine biosynthetic process / polyamine catabolic process / polyamine metabolic process / small molecule metabolic process / spermine catabolic process / xenobiotic metabolic process
Components
cytoplasm / cytosol / nucleus
General Function
Spermine:oxygen oxidoreductase (spermidine-forming) activity
Specific Function
Flavoenzyme which catalyzes the oxidation of spermine to spermidine. Can also use N(1)-acetylspermine and spermidine as substrates, with different affinity depending on the isoform (isozyme) and on the experimental conditions. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs. May contribute to beta-alanine production via aldehyde dehydrogenase conversion of 3-amino-propanal.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0010393|Spermine oxidase (SMOX)
ATGCAAAGTTGTGAATCCAGTGGTGACAGTGCGGATGACCCTCTCAGTCGCGGCCTACGG
AGAAGGGGACAGCCTCGTGTGGTGGTGATCGGCGCCGGCTTGGCTGGCCTGGCTGCAGCC
AAAGCACTTCTTGAGCAGGGTTTCACGGATGTCACTGTGCTTGAGGCTTCCAGCCACATC
GGAGGCCGTGTGCAGAGTGTGAAACTTGGACACGCCACCTTTGAGCTGGGAGCCACCTGG
ATCCATGGCTCCCATGGGAACCCTATCTATCATCTAGCAGAAGCCAACGGCCTCCTGGAA
GAGACAACCGATGGGGAACGCAGCGTGGGCCGCATCAGCCTCTATTCCAAGAATGGCGTG
GCCTGCTACCTTACCAACCACGGCCGCAGGATCCCCAAGGACGTGGTTGAGGAATTCAGC
GATTTATACAACGAGGTCTATAACTTGACCCAGGAGTTCTTCCGGCACGATAAACCAGTC
AATGCTGAAAGTCAAAATAGCGTGGGGGTGTTCACCCGAGAGGAGGTGCGTAACCGCATC
AGGAATGACCCTGACGACCCAGAGGCTACCAAGCGCCTGAAGCTCGCCATGATCCAGCAG
TACCTGAAGGTGGAGAGCTGTGAGAGCAGCTCACACAGCATGGACGAGGTGTCCCTGAGC
GCCTTCGGGGAGTGGACCGAGATCCCCGGCGCTCACCACATCATCCCCTCGGGCTTCATG
CGGGTTGTGGAGCTGCTGGCGGAGGGCATCCCTGCCCACGTCATCCAGCTAGGGAAACCT
GTCCGCTGCATTCACTGGGACCAGGCCTCAGCCCGCCCCAGAGGCCCTGAGATTGAGCCC
CGGGGTGAGGGCGACCACAATCACGACACTGGGGAGGGTGGCCAGGGTGGAGAGGAGCCC
CGGGGGGGCAGGTGGGATGAGGATGAGCAGTGGTCGGTGGTGGTGGAGTGCGAGGACTGT
GAGCTGATCCCGGCGGACCATGTGATTGTGACCGTGTCGCTAGGTGTGCTAAAGAGGCAG
TACACCAGTTTCTTCCGGCCAGGCCTGCCCACAGAGAAGGTGGCTGCCATCCACCGCCTG
GGCATTGGCACCACCGACAAGATCTTTCTGGAATTCGAGGAGCCCTTCTGGGGCCCTGAG
TGCAACAGCCTACAGTTTGTGTGGGAGGACGAAGCAGAGAGCCACACCCTCACCTACCCA
CCTGAGCTCTGGTACCGCAAGATCTGCGGCTTTGATGTCCTCTACCCGCCTGAGCGCTAC
GGCCATGTGCTGAGCGGCTGGATCTGCGGGGAGGAGGCCCTCGTCATGGAGAAGTGTGAT
GACGAGGCAGTGGCCGAGATCTGCACGGAGATGCTGCGTCAGTTCACAGGGAACCCCAAC
ATTCCAAAACCTCGGCGAATCTTGCGCTCGGCCTGGGGCAGCAACCCTTACTTCCGCGGC
TCCTATTCATACACGCAGGTGGGCTCCAGCGGGGCGGATGTGGAGAAGCTGGCCAAGCCC
CTGCCGTACACAGAGAGCTCAAAGACAGCGCATGGAAGCTCCACAAAGCAGCAGCCTGGT
CACCTTTTCTCTTCCAAGTGCCCAGAACAGCCCCTGGATGCTAACAGGGGCGCCGTAAAG
CCCATGCAGGTGCTGTTTTCCGGTGAGGCCACCCACCGCAAGTACTATTCCACCACCCAC
GGTGCTCTGCTGTCCGGCCAGCGTGAGGCTGCCCGCCTCATTGAGATGTACCGAGACCTC
TTCCAGCAGGGGACCTGA
Chromosome Location
20
Locus
20p13
External Identifiers
ResourceLink
UniProtKB IDQ9NWM0
UniProtKB Entry NameSMOX_HUMAN
GenBank Protein ID14860862
GenBank Gene IDAY033889
GenAtlas IDSMOX
HGNC IDHGNC:15862
General References
  1. Wang Y, Devereux W, Woster PM, Stewart TM, Hacker A, Casero RA Jr: Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure. Cancer Res. 2001 Jul 15;61(14):5370-3. [Article]
  2. Murray-Stewart T, Wang Y, Devereux W, Casero RA Jr: Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics. Biochem J. 2002 Dec 15;368(Pt 3):673-7. [Article]
  3. Murray-Stewart T, Wang Y, Goodwin A, Hacker A, Meeker A, Casero RA Jr: Nuclear localization of human spermine oxidase isoforms - possible implications in drug response and disease etiology. FEBS J. 2008 Jun;275(11):2795-806. doi: 10.1111/j.1742-4658.2008.06419.x. Epub 2008 Apr 17. [Article]
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  9. Wang Y, Murray-Stewart T, Devereux W, Hacker A, Frydman B, Woster PM, Casero RA Jr: Properties of purified recombinant human polyamine oxidase, PAOh1/SMO. Biochem Biophys Res Commun. 2003 May 16;304(4):605-11. [Article]
  10. Vujcic S, Diegelman P, Bacchi CJ, Kramer DL, Porter CW: Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin. Biochem J. 2002 Nov 1;367(Pt 3):665-75. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00127Spermineexperimental, nutraceuticalyesligandDetails
DB04188MDL72527experimentalunknowninhibitorDetails