Anti-Spermine synthase antibody [EPR9252(B)] - BSA and Azide free

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Spermine synthase also recognized as SMS is an enzyme that catalyzes the conversion of spermidine to spermine. Mechanically it transfers an aminopropyl group from decarboxylated S-adenosylmethionine to spermidine resulting in spermine. This enzyme is around 43 kDa in size and is ubiquitously expressed in various tissues with notable expression in the liver and kidney. It plays an essential role in the polyamine biosynthetic pathway contributing to cellular growth and differentiation.

Biological function summary

The enzyme fosters cellular functions by modulating spermine levels which are necessary for stabilizing DNA RNA and ribosome structures. It does not exist as part of a larger complex but works closely with other enzymes in the polyamine synthesis process. Spermine contributes to cellular homeostasis influencing ion channel activity and defending against oxidative stress. The balanced production of spermine by spermine synthase represents its importance in maintaining normal cellular physiology.

Pathways

Spermine synthase plays an important role in the polyamine metabolic pathway converting spermidine to spermine finalizing the chain of polyamine biosynthesis. It interacts closely with enzymes like ornithine decarboxylase which facilitates the initial steps of polyamine synthesis and spermidine synthase which precedes spermine formation. The pathway is fundamental to cell proliferation apoptosis and differentiation processes emphasizing the enzyme's pivotal part in cell biology.

Associated diseases and disorders

Alterations in spermine synthase activity associate with Snyder-Robinson syndrome and cancer. Snyder-Robinson syndrome connected to mutations in the SMS gene results in neurodevelopmental difficulties and skeletal abnormalities. In cancer dysregulation of polyamine synthesis where spermine synthase is implicated contributes to uncontrolled cellular proliferation. Changes in spermine levels impact other proteins including ornithine decarboxylase and other polyamine pathway enzymes which participate in disease progression.