Polyamine metabolic enzyme

Polyamine metabolic enzymes are a group of enzymes responsible for the biosynthesis, interconversion, and catabolism of natural polyamines such as putrescine, spermidine, and spermine—key molecules essential for cell proliferation, gene expression, and metabolic regulation[1][2][5][7][9]. Key enzymes include ornithine decarboxylase (ODC), S-adenosylmethionine decarboxylase (AdoMetDC), spermidine synthase, spermine synthase, spermine oxidase (SMOX), polyamine oxidases, and acetyltransferases[3][4][5][9]. These enzymes regulate polyamine levels by catalyzing specific steps in their synthesis (from amino acid precursors), interconversion, or breakdown pathways. Polyamine metabolic enzymes are considered promising therapeutic targets, particularly in cancer, due to the reliance of rapidly proliferating cells on elevated polyamine biosynthesis and uptake. Drugs targeting these enzymes (especially ODC inhibitors like eflornithine) have reached clinical use or late-stage trials for oncology and tropical disease indications. Because this entry refers to a class of enzymes rather than a single molecular entity, it is considered too broad or non-canonical for assignments regarding a single "target".

Other names

Polyamine metabolism enzymeEnzymes of polyamine metabolismPolyamine pathway enzymePolyamine metabolic enzymes (incorrect plural)

Inhibition of ornithine decarboxylase to deplete polyamine synthesis; Inhibition of S-adenosylmethionine decarboxylase; Blockade of polyamine uptake transporters; Induction of cytotoxicity via polyamine analogs; Inhibition of polyamine oxidases to reduce catabolism