protein-cysteine S-palmitoyltransferase activity

Definition

Target type: molecularfunction

Catalysis of the transfer of a palmitoyl (systematic name, hexadecanoyl) group to a sulfur atom on the cysteine of a protein molecule, in the reaction hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]. [GOC:ai, GOC:pr, RHEA:36683]

Protein-cysteine S-palmitoyltransferase activity refers to the enzymatic process of attaching a palmitic acid molecule, a 16-carbon saturated fatty acid, to a cysteine residue within a protein. This process, known as palmitoylation, is a type of lipid modification that plays a crucial role in regulating protein function and cellular localization. Palmitoyltransferases, the enzymes responsible for this reaction, recognize specific cysteine residues within target proteins based on their sequence context and local structure. The palmitic acid molecule is transferred from a palmitoyl-CoA donor molecule to the cysteine residue, forming a thioester linkage. This addition of palmitic acid can alter the protein's hydrophobicity, its interaction with membranes, its stability, and its ability to interact with other proteins. Palmitoylation is a dynamic process, meaning that the palmitic acid can be removed from the protein by palmitoylthioesterases, allowing for reversible regulation of protein function. This reversible modification allows for rapid and localized control of protein activity and localization in response to cellular cues. The diverse effects of palmitoylation contribute to its involvement in a wide range of cellular processes, including signal transduction, membrane trafficking, protein folding, and cytoskeletal organization.'
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Proteins (2)

Compounds (2)