| Tbio | Spermine oxidase |
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.
Polyamines are ubiquitous polycationic alkylamines which include spermine, spermidine, putrescine, and agmatine. These molecules participate in a broad range of cellular functions which include cell cycle modulation, scavenging reactive oxygen species, and the control of gene expression. These molecules also play important roles in neurotransmission through their regulation of cell-surface receptor activity, involvement in intracellular signalling pathways, and their putative roles as neurotransmitters. This gene encodes an FAD-containing enzyme that catalyzes the oxidation of spermine to spermadine and secondarily produces hydrogen peroxide. Multiple transcript variants encoding different isoenzymes have been identified for this gene, some of which have failed to demonstrate significant oxidase activity on natural polyamine substrates. The characterized isoenzymes have distinctive biochemical characteristics and substrate specificities, suggesting the existence of additional levels of complexity in polyamine catabolism. [provided by RefSeq, Jul 2012]
Polyamines are ubiquitous polycationic alkylamines which include spermine, spermidine, putrescine, and agmatine. These molecules participate in a broad range of cellular functions which include cell cycle modulation, scavenging reactive oxygen species, and the control of gene expression. These molecules also play important roles in neurotransmission through their regulation of cell-surface receptor activity, involvement in intracellular signalling pathways, and their putative roles as neurotransmitters. This gene encodes an FAD-containing enzyme that catalyzes the oxidation of spermine to spermadine and secondarily produces hydrogen peroxide. Multiple transcript variants encoding different isoenzymes have been identified for this gene, some of which have failed to demonstrate significant oxidase activity on natural polyamine substrates. The characterized isoenzymes have distinctive biochemical characteristics and substrate specificities, suggesting the existence of additional levels of complexity in polyamine catabolism. [provided by RefSeq, Jul 2012]
Comments
| Disease | Target Count |
|---|---|
| Cerebrovascular accident | 63 |
| Mood Disorders | 184 |
| Disease | Target Count | P-value |
|---|---|---|
| psoriasis | 6694 | 1.6e-08 |
| medulloblastoma, large-cell | 6241 | 3.4e-06 |
| malignant mesothelioma | 3232 | 8.8e-06 |
| atypical teratoid / rhabdoid tumor | 5112 | 5.1e-05 |
| group 3 medulloblastoma | 4104 | 1.7e-04 |
| adult high grade glioma | 3801 | 4.4e-04 |
| ependymoma | 4679 | 9.6e-04 |
| glioblastoma | 5792 | 1.4e-03 |
| non primary Sjogren syndrome sicca | 891 | 1.4e-02 |
| osteosarcoma | 7950 | 2.7e-02 |
| oligodendroglioma | 2850 | 3.2e-02 |
| Disease | Target Count | Z-score | Confidence |
|---|---|---|---|
| Panic disorder | 61 | 0.0 | 0.9 |
| Disease | log2 FC | p |
|---|---|---|
| adult high grade glioma | -1.200 | 4.4e-04 |
| atypical teratoid / rhabdoid tumor | -1.100 | 5.1e-05 |
| ependymoma | 1.100 | 9.6e-04 |
| glioblastoma | -1.100 | 1.4e-03 |
| group 3 medulloblastoma | -1.500 | 1.7e-04 |
| malignant mesothelioma | -1.500 | 8.8e-06 |
| medulloblastoma, large-cell | -1.300 | 3.4e-06 |
| non primary Sjogren syndrome sicca | 1.100 | 1.4e-02 |
| oligodendroglioma | 1.200 | 3.2e-02 |
| osteosarcoma | 1.141 | 2.7e-02 |
| psoriasis | 1.500 | 1.6e-08 |
MQSCESSGDSADDPLSRGLRRRGQPRVVVIGAGLAGLAAAKALLEQGFTDVTVLEASSHIGGRVQSVKLG 1 - 70 HATFELGATWIHGSHGNPIYHLAEANGLLEETTDGERSVGRISLYSKNGVACYLTNHGRRIPKDVVEEFS 71 - 140 DLYNEVYNLTQEFFRHDKPVNAESQNSVGVFTREEVRNRIRNDPDDPEATKRLKLAMIQQYLKVESCESS 141 - 210 SHSMDEVSLSAFGEWTEIPGAHHIIPSGFMRVVELLAEGIPAHVIQLGKPVRCIHWDQASARPRGPEIEP 211 - 280 RGEGDHNHDTGEGGQGGEEPRGGRWDEDEQWSVVVECEDCELIPADHVIVTVSLGVLKRQYTSFFRPGLP 281 - 350 TEKVAAIHRLGIGTTDKIFLEFEEPFWGPECNSLQFVWEDEAESHTLTYPPELWYRKICGFDVLYPPERY 351 - 420 GHVLSGWICGEEALVMEKCDDEAVAEICTEMLRQFTGNPNIPKPRRILRSAWGSNPYFRGSYSYTQVGSS 421 - 490 GADVEKLAKPLPYTESSKTAPMQVLFSGEATHRKYYSTTHGALLSGQREAARLIEMYRDLFQQGT 491 - 555 //
