Polyamine metabolic enzymes

Polyamine metabolic enzymes represent a critical set of proteins that regulate the intracellular concentrations of polyamines, including putrescine, spermidine, and spermine (Casero et al., 2018, Nature Reviews Cancer). These enzymes, such as ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (SAMDC), are essential for cell growth, differentiation, and survival due to the role of polyamines in stabilizing DNA structure and facilitating protein synthesis (Pegg, 2016, IUBMB Life). In many cancers, the polyamine pathway is upregulated to support rapid proliferation, making these enzymes attractive therapeutic targets (Wallace et al., 2003, Biochem J). Eflornithine, an irreversible inhibitor of ODC, is a prominent drug in this class, recently approved by the FDA to reduce the risk of relapse in adult and pediatric patients with high-risk neuroblastoma (FDA, 2023). Beyond oncology, these enzymes are targeted in infectious diseases like African sleeping sickness, where parasite-specific polyamine metabolism is disrupted (Heby et al., 2007, Amino Acids). Therapeutic strategies include direct enzyme inhibition, the use of polyamine mimetics to trigger feedback inhibition, and the induction of catabolic enzymes like spermidine/spermine N1-acetyltransferase (SSAT) to deplete cellular polyamine pools.

Other names

Polyamine metabolic pathway enzymesPolyamine biosynthetic enzymesPolyamine catabolic enzymesOrnithine decarboxylase (ODC)S-adenosylmethionine decarboxylase (SAMDC)Spermidine/spermine N1-acetyltransferase (SSAT)Spermine oxidase (SMOX)

Inhibition of rate-limiting biosynthetic enzymes (ODC, SAMDC) or induction of catabolic enzymes (SSAT) to deplete intracellular polyamine levels and inhibit cell growth (Casero et al., 2018).