Protein Methylase II, also known as protein arginine methyltransferase 2 (PRMT2), is an enzyme involved in post-translational modification of proteins. It belongs to the family of protein arginine methyltransferases (PRMTs), which catalyze the transfer of a methyl group from S-adenosylmethionine (SAM) to the guanidine nitrogen atom of specific arginine residues in protein substrates.
Protein Methylase II plays a crucial role in the regulation of gene expression, chromatin remodeling, and signal transduction pathways by adding methyl groups to specific arginine residues in target proteins. This modification can affect protein-protein interactions, protein stability, and subcellular localization. PRMT2 primarily catalyzes the formation of symmetric dimethylarginine (sDMA) residues, which have been implicated in various cellular processes, including RNA processing, DNA repair, and protein translation.
The activity of Protein Methylase II is tightly regulated, and dysregulation of PRMT2 has been implicated in several diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. It has been demonstrated that altered PRMT2 expression or activity can lead to dysregulated gene expression and aberrant signaling pathways, contributing to the development and progression of various diseases.
In summary, Protein Methylase II is an enzyme that catalyzes the addition of methyl groups to arginine residues in protein substrates. It plays a critical role in the regulation of cellular processes and its dysregulation is associated with multiple diseases.
