Polyamine catabolic enzyme

Polyamine catabolic enzymes facilitate the breakdown of cellular polyamines such as spermidine and spermine. The main enzymes in this group—spermidine/spermine N¹-acetyltransferase (SSAT), spermine oxidase (SMO), and N¹-acetylpolyamine oxidase (APAO)—work sequentially or in parallel to acetylate and oxidize polyamines, thus regulating their intracellular levels and linking modified polyamines to further metabolic processes or excretion. These enzymes play pivotal roles in maintaining polyamine homeostasis and are tightly regulated in response to both physiological and pathological stimuli. Aberrant activation or inhibition of these enzymes can lead to altered cell proliferation, apoptosis, oxidative stress, and is implicated in diseases such as cancer, inflammation, neurodegeneration, and aging. Therapeutic interventions either aim to inhibit excessive polyamine catabolic activity or exploit their upregulation to induce cytotoxicity in proliferative diseases such as cancer[1][3][4][5].

Other names

Spermidine/spermine N¹-acetyltransferase (SSAT)Spermine oxidase (SMO)N¹-acetylpolyamine oxidase (APAO)Polyamine oxidase (PAO)Polyamine degrading enzymes

Drugs targeting these enzymes may induce, inhibit, or modulate enzymatic activity, leading to polyamine depletion, accumulation of toxic metabolites (such as hydrogen peroxide and aldehydes), cellular stress, and cell death[4][5][1]. Inhibition decreases tumor cell proliferation; induction can promote cell death through oxidative stress.