N-terminal peptidyl-glycine methylation

Definition

Target type: biologicalprocess

The methylation of the N-terminal glycine of proteins to form the derivative N-methylglycine. [RESID:AA0063]

N-terminal peptidyl-glycine methylation is a post-translational modification that involves the addition of a methyl group to the nitrogen atom of the glycine residue at the N-terminus of a protein. This process is catalyzed by a specific enzyme, N-terminal glycine methyltransferase (NGMT). NGMT utilizes S-adenosyl methionine (SAM) as a methyl donor. The reaction proceeds in two steps:

1. **Formation of a Schiff base intermediate:** The amino group of the N-terminal glycine forms a Schiff base with the pyridoxal phosphate cofactor of NGMT.

2. **Methyl transfer:** The methyl group from SAM is transferred to the nitrogen atom of the glycine residue.

This methylation event can affect various aspects of protein function, including:

* **Protein stability and folding:** Methylation can influence the conformation and stability of the protein by modifying the interactions between the N-terminal glycine and other residues.

* **Protein-protein interactions:** The modification can alter the binding affinity of the protein to its interacting partners.

* **Cellular localization:** Methylation can influence the trafficking and localization of the protein within the cell.

N-terminal peptidyl-glycine methylation is a widespread modification found in a variety of organisms, including bacteria, yeast, plants, and animals. This modification plays an important role in diverse biological processes such as signal transduction, gene regulation, and cell growth. In humans, NGMT is involved in the biosynthesis of leukotrienes, a class of inflammatory mediators.

While the exact biological roles of N-terminal peptidyl-glycine methylation are still being elucidated, it is a crucial modification that affects many aspects of protein function and cellular processes.'
"

Proteins (1)

Compounds (1)