EC 1.5.3.13 - N1-acetylpolyamine oxidase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 1.5.3.13

Names

Accepted name:
N1-acetylpolyamine oxidase
Other names:
hPAO-1
PAO [ambiguous]
mPAO
hPAO
polyamine oxidase [ambiguous]
Systematic name:
N1-acetylpolyamine:oxygen oxidoreductase (3-acetamidopropanal-forming)

Reactions

Cofactor

Comments:

The enzyme also catalyses the reaction: N1,N12-diacetylspermine + O2 + H2O = N1-acetylspermidine + 3-acetamamidopropanal + H2O2 [1]. No or very weak activity with spermine, or spermidine in absence of aldehydes. In presence of aldehydes the enzyme catalyses the reactions: 1. spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2, and with weak efficiency 2. spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2 [2]. A flavoprotein (FAD). This enzyme, encoded by the PAOX gene, is found in mammalian peroxisomes and oxidizes N1-acetylated polyamines at the exo (three-carbon) side of the secondary amine, forming 3-acetamamidopropanal. Since the products of the reactions are deacetylated polyamines, this process is known as polyamine back-conversion. Differs in specificity from EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.15 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0052899 , GO:0052904 , GO:0052903 , GO:0052902 , GO:0052901
UniProtKB/Swiss-Prot:

References

  1. Vujcic, S., Liang, P., Diegelman, P., Kramer, D. L., Porter, C. W.
    Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion.
    Biochem. J. 370: 19-28 (2003). [PMID: 12477380]
  2. Jarvinen, A., Grigorenko, N., Khomutov, A. R., Hyvonen, M. T., Uimari, A., Vepsalainen, J., Sinervirta, R., Keinanen, T. A., Vujcic, S., Alhonen, L., Porter, C. W., Janne, J.
    Metabolic stability of alpha-methylated polyamine derivatives and their use as substitutes for the natural polyamines.
    J. Biol. Chem. 280: 6595-6601 (2005). [PMID: 15611107]
  3. Wang, Y., Hacker, A., Murray-Stewart, T., Frydman, B., Valasinas, A., Fraser, A. V., Woster, P. M., Casero, R. A.
    Properties of recombinant human N1-acetylpolyamine oxidase (hPAO): potential role in determining drug sensitivity.
    Cancer Chemother. Pharmacol. 56: 83-90 (2005). [PMID: 15791459]
  4. Wu, T., Yankovskaya, V., McIntire, W. S.
    Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase.
    J. Biol. Chem. 278: 20514-20525 (2003). [PMID: 12660232]

[EC 1.5.3.13 created 2009]