SMOX
SMOX (spermine oxidase, also known as SMO, PAO, PAOh1 and C20orf16) is a flavin-dependent enzyme that oxidises spermine to spermidine. It helps set intracellular polyamine concentrations and belongs to the flavin monoamine oxidase family. Browse Assay Genie's current range of SMOX research reagents below, or read on for the biology behind the target.
SMOX is a flavoenzyme that catalyses the oxidation of spermine to spermidine, secondarily producing hydrogen peroxide. It can also use N(1)-acetylspermine and spermidine as substrates, with an affinity that depends on the isoform and on the experimental conditions. Through this activity SMOX plays an important role in regulating intracellular polyamine concentration. It has also been described as a potential determinant of cellular sensitivity to antitumour polyamine analogues, and it may contribute to beta-alanine production through aldehyde dehydrogenase conversion of 3-amino-propanal.
Polyamines such as spermine, spermidine, putrescine and agmatine are ubiquitous polycationic alkylamines. They take part in cell cycle modulation, scavenging of reactive oxygen species and control of gene expression. They also contribute to neurotransmission by regulating cell-surface receptor activity, by involvement in intracellular signalling pathways and by putative roles as neurotransmitters. The SMOX gene encodes an FAD-containing enzyme, and the protein is found in the cytoplasm and the nucleus. It belongs to the flavin monoamine oxidase family and to the HGNC gene groups of flavoproteins and polyamine oxidases. The mouse ortholog is Smox.
Multiple transcript variants encode different isoenzymes. The characterised isoenzymes differ in their biochemical properties and substrate specificities, and some variants have not shown significant oxidase activity on natural polyamine substrates. This suggests further levels of complexity in polyamine catabolism. Researchers working with the SMOX gene or SMOX protein therefore often need to consider which isoform is being studied. The gene was previously named chromosome 20 open reading frame 16 (C20orf16), and the aliases FLJ20746, dJ779E11.1, MGC1010, SMO and PAO also appear in the literature.
SMOX converts spermine to spermidine and helps regulate intracellular polyamine concentration, making it a central enzyme for studying polyamine homeostasis.
SMOX has the potential to act as a determinant of cellular sensitivity to antitumour polyamine analogues, which links it to this area of drug response research.
The SMOX reaction secondarily produces hydrogen peroxide, while polyamines themselves take part in scavenging reactive oxygen species.
Transcript variants encode isoenzymes with distinct substrate specificities, so SMOX is a useful subject for studying complexity in polyamine metabolism.
SMOX is a flavoenzyme that catalyses the oxidation of spermine to spermidine, and secondarily produces hydrogen peroxide. It can also act on N(1)-acetylspermine and spermidine, depending on isoform and conditions. In this way it regulates intracellular polyamine concentration.
SMOX is also called SMO, PAO, PAOh1, C20orf16, FLJ20746, dJ779E11.1 and MGC1010. Multiple transcript variants encode different isoenzymes with distinct substrate specificities, and some showed no significant oxidase activity on natural polyamine substrates.
A mouse ortholog, Smox, is recorded for the human gene. SMOX belongs to the flavin monoamine oxidase family and to the polyamine oxidase gene group. Check the datasheet of any product for its validated reactivity.
Other polyamine metabolism enzymes and flavin monoamine oxidase family members that are studied alongside SMOX.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9NWM0; product specifications from Assay Genie datasheets.