S-adenosylmethionine-dependent methyltransferase

S-adenosylmethionine-dependent methyltransferases are a large and evolutionary conserved family of enzymes that utilize S-adenosyl-L-methionine (SAM or AdoMet) as a methyl group donor to catalyze the methylation of diverse substrates, including DNA, RNA, proteins, polysaccharides, lipids, and small-molecule metabolites. These enzymes play essential roles in epigenetic regulation, signal transduction, metabolic biosynthesis, and cellular homeostasis. Aberrant activity of specific methyltransferases is implicated in various diseases, most notably cancer and neurodegenerative disorders, making certain family members (such as DNA methyltransferases) important therapeutic targets. Methyltransferases share structural motifs such as the Rossmann fold and a conserved catalytic site but exhibit a wide range of substrate specificities and biological roles[2][3][5]. Drugs targeting S-adenosylmethionine-dependent methyltransferases generally function by inhibiting methyl group transfer to the target biomolecule, most therapeutically in the context of abnormal DNA methylation states seen in cancers[3]. Disruption of methyltransferase activity can have broad biological consequences due to the enzymes’ ubiquitous presence and essential functions.

Other names

SAM-dependent methyltransferaseAdoMet-dependent methyltransferaseS-adenosyl-L-methionine-dependent methyltransferase

Inhibition of methyl group transfer, leading to hypomethylation of DNA/RNA/protein Blockade of cofactor (SAM) binding Suicide inhibition (for certain drugs, e.g., Decitabine)