Polyamine synthesis pathway enzyme

Polyamine synthesis pathway enzymes are a group of enzymes that catalyze the biosynthesis of polyamines such as putrescine, spermidine, and spermine from amino acid precursors (mainly arginine, ornithine, and methionine)[1][5][6]. The pathway's key enzymes include arginase (converts arginine to ornithine), ornithine decarboxylase (ODC) (converts ornithine to putrescine), S-adenosylmethionine decarboxylase (AdoMetDC) (produces decarboxylated SAM for aminopropyl transfer), spermidine synthase and spermine synthase (catalyze the formation of spermidine and spermine respectively)[1][5][6]. These enzymes are critical regulators of cell proliferation, differentiation, gene expression, and are upregulated in various cancers, making several pathway members validated therapeutic targets[5]. Inhibition of these enzymes can arrest cell cycle progression and induce apoptosis, with ODC being the clinically most relevant target for small molecule inhibition, such as by eflornithine (DFMO)[5][6]. Aberrant regulation of polyamine metabolism is implicated in multiple diseases, most notably cancer, but also impacts neurodegeneration and cardiovascular disorders due to the fundamental roles of polyamines in cell and tissue homeostasis[1][5][6]. Note: For database entries, each of the main enzymes (e.g., "Ornithine decarboxylase", "S-adenosylmethionine decarboxylase") should have their own canonical record. This answer covers the pathway ensemble as requested but indicates this is not a canonical target form[1][5][6].

Other names

Polyamine biosynthetic enzymesPolyamine metabolic enzymes

Enzyme inhibition (e.g., ODC inhibition leading to decreased polyamine synthesis) Targeting polyamine homeostasis or metabolism Polyamine analog competition