protein-arginine N-methyltransferase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: S-adenosyl-L-methionine + (protein)-arginine = S-adenosyl-L-homocysteine + (protein)-N-methyl-arginine. [GOC:mah, PMID:12351636, PMID:31284549]

Protein-arginine N-methyltransferase activity refers to the enzymatic ability to catalyze the transfer of a methyl group from a donor molecule, such as S-adenosyl methionine (SAM), to the guanidino nitrogen of arginine residues within a protein substrate. This methylation reaction is a critical post-translational modification that can significantly alter the structure, function, and interactions of proteins.

The molecular function of protein-arginine N-methyltransferases involves a multi-step process. First, the enzyme binds to both the protein substrate and the SAM cofactor. The SAM molecule is then positioned in the active site of the enzyme, where its methyl group is transferred to the target arginine residue. This transfer is facilitated by the enzyme's catalytic residues and is accompanied by the release of S-adenosyl homocysteine (SAH) as a byproduct.

The methylation of arginine residues can have a variety of effects on protein function. For instance, it can:

- Alter protein-protein interactions by creating new binding sites or masking existing ones.
- Modulate protein stability and folding.
- Influence enzymatic activity by affecting the conformation of the active site.
- Regulate protein localization and trafficking.

Protein-arginine N-methyltransferases play important roles in a wide range of cellular processes, including:

- Signal transduction pathways
- Gene expression regulation
- Chromatin remodeling
- Immune responses
- Cell growth and differentiation

Dysregulation of protein-arginine N-methyltransferase activity has been implicated in various diseases, including cancer, neurodegenerative disorders, and autoimmune diseases. This highlights the crucial role of these enzymes in maintaining cellular homeostasis and the potential for therapeutic interventions targeting their activity.'
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Proteins (10)

Compounds (25)