palmitoyltransferase activity

Definition

Target type: molecularfunction

Catalysis of the transfer of a palmitoyl (CH3-[CH2]14-CO-) group to an acceptor molecule. [GOC:ai]

Palmitoyltransferase activity is a crucial enzymatic process that involves the attachment of palmitic acid, a 16-carbon saturated fatty acid, to a specific target molecule. This covalent modification, known as palmitoylation, plays a vital role in regulating the function, localization, and stability of a diverse array of cellular proteins. The palmitoyltransferase enzymes catalyze the transfer of the palmitate moiety from a donor molecule, typically palmitoyl-CoA, to the target protein. This transfer typically occurs at cysteine residues within the protein, forming a thioester bond. The location and extent of palmitoylation can significantly influence the protein's interactions with other molecules, its membrane association, and its overall activity. In many cases, palmitoylation acts as a reversible "on-off" switch, modulating protein function in response to cellular signals. The diverse range of palmitoylated proteins highlights the broad impact of this modification on cellular processes. For instance, palmitoylation is involved in regulating signal transduction pathways, protein trafficking, membrane organization, and cellular adhesion. Dysregulation of palmitoylation has been implicated in various diseases, including cancer, neurodegenerative disorders, and metabolic syndromes, emphasizing the importance of understanding this critical molecular function.'
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Proteins (2)

Compounds (1)