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Related Experiment Video

Updated: May 30, 2026

Efficient Purification and LC-MS/MS-based Assay Development for Ten-Eleven Translocation-2 5-Methylcytosine Dioxygenase

Efficient Purification and LC-MS/MS-based Assay Development for Ten-Eleven Translocation-2 5-Methylcytosine Dioxygenase

Published on: October 15, 2018

Spermine oxidase: ten years after.

Manuela Cervelli¹, Roberto Amendola, Fabio Polticelli

¹Department of Biology, University Roma Tre, 00146, Rome, Italy. cervelli@uniroma3.it

|August 3, 2011

Summary

Spermine oxidase (SMO) is a key enzyme in polyamine metabolism. Its dysregulation impacts cell functions and disease, highlighting its role in health and pathology.

Area of Science:

Biochemistry
Molecular Biology
Cellular Physiology

Background:

Spermine oxidase (SMO) is a recently discovered FAD-dependent enzyme crucial for mammalian polyamine catabolism.
SMO specifically oxidizes spermine (Spm), a vital molecule for DNA synthesis, proliferation, and cellular signaling.

Purpose of the Study:

To review 10 years of research on Spermine oxidase (SMO).
To cover the biochemical, cellular, and physiological roles of SMO.
To explore SMO's involvement in drug response, apoptosis, and diseases like cancer.

Main Methods:

Literature review of scientific research on Spermine oxidase (SMO).

Main Results:

SMO activity produces spermidine, hydrogen peroxide (H2O2), and 3-aminopropanal, which can cause cellular damage.

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SMO deregulation alters polyamine homeostasis, contributing to various pathological conditions.

SMO is a highly inducible enzyme implicated in cancer and cellular stress responses.

Conclusions:

Spermine oxidase (SMO) plays a significant role in polyamine metabolism and homeostasis.
Dysregulation of SMO and its products are linked to cellular damage and disease etiology.
Further research into SMO is essential for understanding its broad physiological and pathological implications.