N-terminal peptidyl-serine dimethylation

Definition

Target type: biologicalprocess

The dimethylation of the N-terminal serine of proteins to form the derivative N,N-dimethylserine. [PMID:20668449]

N-terminal peptidyl-serine dimethylation is a post-translational modification that involves the addition of two methyl groups to the nitrogen atom of the serine residue at the N-terminus of a protein. This modification is catalyzed by a specific class of enzymes known as N-terminal peptidyl-serine dimethyltransferases (N-PSMTs).

The process typically begins with the recognition of a specific N-terminal sequence by the N-PSMT. This sequence often contains a serine residue followed by a glycine residue (Ser-Gly). The N-PSMT then binds to the substrate protein and utilizes S-adenosyl methionine (SAM) as a methyl donor.

The N-PSMT catalyzes the transfer of the methyl group from SAM to the nitrogen atom of the serine residue. This reaction is repeated twice, resulting in the addition of two methyl groups to the serine residue.

N-terminal peptidyl-serine dimethylation can have a variety of effects on protein function, depending on the specific protein and its location within the cell. In some cases, this modification can enhance protein stability or regulate protein-protein interactions. In other cases, it can influence protein localization or activity.

For example, N-terminal peptidyl-serine dimethylation has been shown to play a role in the regulation of cell signaling pathways, such as the Wnt signaling pathway. It has also been implicated in the development of certain types of cancer.

In summary, N-terminal peptidyl-serine dimethylation is a complex post-translational modification that can significantly impact protein function. Further research is ongoing to elucidate the full scope of this modification and its implications for cellular processes.'
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Proteins (1)

Compounds (1)