protein-arginine omega-N symmetric methyltransferase activity

Definition

Target type: molecularfunction

Catalysis of the addition of a second methyl group to methylated peptidyl-arginine. Methylation is on the terminal nitrogen (omega nitrogen) residue that is not already methylated, resulting in symmetrical peptidyl-N(omega),N'(omega)-dimethyled arginine residues. [EC:2.1.1.320, PMID:14705965, RESID:AA0067, RESID:AA0069]

Protein-arginine omega-N symmetric methyltransferase activity refers to the enzymatic process by which a methyl group is transferred from a donor molecule, typically S-adenosyl methionine (SAM), to the omega-nitrogen of an arginine residue within a protein. This methylation event occurs specifically at the terminal nitrogen atom of the guanidino group of arginine, resulting in the formation of monomethylarginine (MMA).

This activity is crucial for a variety of cellular processes, including:

* **Regulation of protein function:** Methylation of arginine residues can alter the structure and conformation of proteins, thereby influencing their activity. This can range from subtle changes in enzyme kinetics to complete inactivation or activation of a protein.
* **Signal transduction:** Methylated arginine residues can act as binding sites for other proteins, facilitating protein-protein interactions and mediating signal transduction pathways.
* **Chromatin remodeling:** Methylation of arginine residues within histone proteins, which package DNA into nucleosomes, plays a crucial role in regulating gene expression. Different methylation patterns can influence chromatin accessibility and the recruitment of specific transcription factors.
* **Cell signaling:** Methylation of arginine residues in various signaling proteins, including kinases and phosphatases, can modulate their activity and downstream signaling pathways.

The enzymes responsible for protein-arginine omega-N symmetric methyltransferase activity belong to a family of methyltransferases known as protein arginine methyltransferases (PRMTs). There are multiple PRMT isoforms, each with distinct substrate specificities and regulatory mechanisms. The different PRMTs generate various methylation products, including monomethylarginine (MMA), symmetric dimethylarginine (SDMA), and asymmetric dimethylarginine (ADMA), each contributing to specific cellular functions.

In summary, protein-arginine omega-N symmetric methyltransferase activity is a fundamental enzymatic process that plays a critical role in regulating various cellular functions through the specific methylation of arginine residues within proteins. This activity is essential for maintaining cellular homeostasis, coordinating signal transduction pathways, and regulating gene expression.'
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Proteins (3)

Compounds (12)