ID:PAOX_MOUSE DESCRIPTION: RecName: Full=Peroxisomal N(1)-acetyl-spermine/spermidine oxidase; EC=1.5.3.13; AltName: Full=Polyamine oxidase; FUNCTION: Flavoenzyme which catalyzes the oxidation of N(1)- acetylspermine to spermidine and is thus involved in the polyamine back-conversion. Can also oxidize N(1)-acetylspermidine to putrescine. Substrate specificity: N(1)-acetylspermine = N(1)- acetylspermidine > N(1),N(12)-diacylspermine >> spermine. Does not oxidize spermidine. 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. CATALYTIC ACTIVITY: N(1)-acetylspermine + O(2) + H(2)O = spermidine + 3-acetamidopropanal + H(2)O(2). CATALYTIC ACTIVITY: N(1)-acetylspermidine + O(2) + H(2)O = putrescine + 3-acetamidopropanal + H(2)O(2). CATALYTIC ACTIVITY: N(1),N(12)-diacetylspermine + O(2) + H(2)O = N(1)-acetylspermidine + 3-acetamidobutanal + H(2)O(2). COFACTOR: Binds 1 FAD per subunit. BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.78 uM for N(1)-acetylspermine; KM=36.8 uM for N(1)-acetylspermidine; KM=716 uM for spermine; KM=150 uM for N(1),N(12)-diacetylspermine; PATHWAY: Amine and polyamine metabolism; spermine metabolism. SUBUNIT: Monomer. SUBCELLULAR LOCATION: Peroxisome (By similarity). Cytoplasm (By similarity). TISSUE SPECIFICITY: Widely expressed at different developmental stages. Expressed at high level in the liver and the stomach, expressed at lower level in heart, spleen, thymus, small intestine, muscle, pancreas, uterus, and breast and expressed at very low level in brain, kidney, lung, testis, skin, adrenal gland and prostate gland. DEVELOPMENTAL STAGE: Expression increased during embryonic development: there is a gradual increase in the tissues on going from 8.5 to 19 day embryos. In the breast, expression is very low in virgin mouse and quite high in pregnant mouse, but decreases in lactating and involuting breasts. INDUCTION: By polyamine analogs. MISCELLANEOUS: Oxidizes N(1)-acetylated polyamines on the exo-side of their N(4)-amino groups. Plant PAO oxidizes spermine on the endo-side of the N(4)-nitrogen (By similarity). MISCELLANEOUS: N-ethylated polyamines are also good substrates for this enzyme: they have been used for cancer clinical trials. They down-regulate polyamine biosynthetic enzymes, but dramatically up- regulate SSAT synthesis, which results in mammalian cells becoming apaptotic. SIMILARITY: Belongs to the flavin monoamine oxidase family.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q8C0L6
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0006598 polyamine catabolic process GO:0008215 spermine metabolic process GO:0009446 putrescine biosynthetic process GO:0009447 putrescine catabolic process GO:0046203 spermidine catabolic process GO:0046208 spermine catabolic process GO:0055114 oxidation-reduction process GO:1901307 positive regulation of spermidine biosynthetic process