serine O-acyltransferase activity

Definition

Target type: molecularfunction

Catalysis of the transfer of an acyl group to an oxygen atom on the serine molecule. [GOC:ai]

Serine O-acyltransferases are a class of enzymes that catalyze the transfer of an acyl group from an acyl donor, such as acetyl-CoA or propionyl-CoA, to the hydroxyl group of serine residues in a protein substrate. This process, known as O-acylation, is a common post-translational modification that can alter the structure, function, and stability of proteins. O-acylation is often involved in regulating protein-protein interactions, cellular signaling pathways, and enzyme activity. The mechanism of serine O-acyltransferase activity typically involves the formation of a covalent intermediate between the enzyme and the acyl donor. The acyl group is then transferred to the hydroxyl group of serine in the substrate protein, resulting in the formation of an ester bond. Serine O-acyltransferases exhibit a wide range of substrate specificity, with some enzymes targeting specific protein substrates while others have broader activity. The activity of these enzymes is often regulated by factors such as phosphorylation, allosteric regulation, and protein-protein interactions. Serine O-acyltransferases play diverse roles in cellular processes, including lipid metabolism, protein trafficking, signal transduction, and gene regulation. Dysregulation of serine O-acyltransferase activity has been implicated in various diseases, including cancer, neurodegenerative disorders, and metabolic disorders.'
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Proteins (1)

Compounds (11)