serine C-palmitoyltransferase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: L-serine + H+ + palmitoyl-CoA = 3-dehydrosphinganine + CO2 + CoA. [EC:2.3.1.50, RHEA:14761]

Serine C-palmitoyltransferase activity is a critical enzymatic function involved in the post-translational modification of proteins by attaching palmitic acid, a saturated fatty acid, to serine residues. This process, known as palmitoylation, plays a vital role in regulating protein localization, stability, and interaction with other molecules.

Palmitoylation is a reversible process, meaning that the palmitic acid can be added or removed from the protein. This reversibility allows for dynamic regulation of protein function and localization.

The addition of palmitic acid to a protein can alter its localization by targeting it to specific cellular membranes, such as the plasma membrane, endoplasmic reticulum, and Golgi apparatus. Palmitoylation can also enhance protein stability by protecting it from degradation. Additionally, palmitoylation can modulate protein-protein interactions by influencing the binding of other proteins to the palmitoylated protein.

Serine C-palmitoyltransferase activity is essential for a wide range of cellular processes, including signal transduction, membrane trafficking, and cell adhesion. It is involved in the regulation of various signaling pathways, including the Wnt, Notch, and Hedgehog pathways. Furthermore, palmitoylation plays a crucial role in the trafficking of proteins to their correct destinations within the cell.

Dysregulation of serine C-palmitoyltransferase activity has been implicated in various diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. Therefore, understanding the molecular mechanisms of serine C-palmitoyltransferase activity is crucial for developing novel therapeutic strategies for these conditions.'
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Proteins (4)

Compounds (1)