METTL13 Inhibitors

Methyltransferase-like 13 (METTL13) is an enzyme that belongs to the class of methyltransferases. These enzymes are involved in transferring a methyl group from a donor molecule, typically S-adenosylmethionine (SAM), to specific substrates. Methyltransferases participate in a wide array of cellular processes by modifying proteins, nucleic acids, and other molecules to regulate their function, stability, or interactions. This post-translational modification can impact protein-protein interactions, protein-DNA interactions, and the overall activity of the modified protein. METTL13, in particular, has been associated with the methylation of specific target proteins, contributing to the modulation of their activities and cellular roles. Inhibitors of METTL13 are molecules designed to interfere with the enzymatic activity of METTL13, preventing it from transferring methyl groups to its target substrates. These inhibitors can either directly bind to the active site of METTL13, obstructing the access of substrates, or they might interact allosterically, altering the enzyme's conformation in a way that reduces its catalytic efficiency. By blocking the function of METTL13, these inhibitors can impact the methylation status of its target proteins, leading to alterations in their functions and interactions. As methyl modifications play pivotal roles in diverse cellular processes, such as signal transduction, gene expression, and protein degradation, understanding the activity and specificity of METTL13 inhibitors can provide significant insights into the broader network of cellular regulation mediated by methylation. Additionally, these inhibitors serve as important tools for dissecting the physiological and molecular roles of METTL13 in various cellular contexts, enriching our comprehension of the intricacies of cellular regulation.