Lysiinimetylaasi

Lysiinimetylaasi is an enzyme that catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (SAM) to the epsilon-amino group of a lysine residue. This post-translational modification is known as lysine methylation. Lysine methylation is a reversible process, and the enzymes responsible for its removal are called lysine demethylases. This modification plays a crucial role in various cellular processes, including gene regulation, protein-protein interactions, and signal transduction.

In eukaryotes, lysine methylation is a prominent modification found on histones, the proteins that package DNA into chromatin. Histone methylation is a key epigenetic mechanism that influences chromatin structure and accessibility, thereby affecting gene transcription. Specific lysine residues on histone tails are targets for methylation by different methyltransferases, leading to either transcriptional activation or repression depending on the specific residue and the degree of methylation. Beyond histones, lysine methylation also occurs on non-histone proteins, impacting their function, localization, and interaction with other molecules.

The activity of lysiinimetylaasi enzymes is tightly regulated, and their dysregulation has been implicated in various diseases, including cancer and neurological disorders. Understanding the mechanisms by which lysiinimetylaasi enzymes function and are regulated is crucial for developing targeted therapies for these conditions. Research in this area continues to uncover new substrates and roles for lysine methylation in cellular physiology and pathology.