5-Amino-1-methylquinolinium (5-Amino-1MQ) selectively targets NNMT, an enzyme linking nicotinamide clearance with S-adenosylmethionine-dependent methylation.[1,2] Inhibition of NNMT by 5-Amino-1MQ allows researchers to explore how altered nicotinamide flux influences NAD⁺ pools, sirtuin activity, epigenetic marks, and metabolic adaptation in cell and animal models.[2–4]
Structural features of 5-Amino-1MQ support active-site binding and competition with NNMT substrates.[1,2] Enzymology assays quantify IC₅₀ values, binding kinetics, and downstream metabolite changes.
In adipocytes and other metabolic tissues, NNMT inhibition has been studied for effects on oxygen consumption, lipolysis, and inflammatory mediators.[2–4] These data facilitate understanding of NNMT as a regulatory node, independent of clinical recommendations.
NNMT overexpression in tumors and other tissues positions 5-Amino-1MQ as a tool for dissecting links between methylation balance, NAD⁺-dependent enzymes, and cellular proliferation, aiding target validation efforts.
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