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S-adenosyl-L-methionine (SAM)-binding proteins and sensors represent a diverse functional class of molecules that utilize or respond to SAM, the primary methyl donor in the cell. This category encompasses a wide array of enzymes, most notably methyltransferases that modify DNA, RNA, proteins, and small molecules, as well as non-enzymatic sensors such as SAM-dependent riboswitches and metabolic regulators like SAMTOR. These proteins play a critical role in epigenetic regulation, signal transduction, and the maintenance of metabolic homeostasis by sensing the availability of methyl groups. In various diseases, particularly cancer and metabolic syndromes, the regulation of SAM-binding proteins is often disrupted, leading to aberrant methylation patterns or metabolic imbalances. While specific methyltransferases are established therapeutic targets, the broader class of 'other' SAM-binding sensors is an emerging area of research for modulating cellular responses to nutrient availability and metabolic stress.
Inhibition of methyltransferase activity or modulation of SAM-sensing riboswitches to alter metabolic flux and gene expression.
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