acyltransferasecatalyzed

Acyltransferase-catalyzed reactions are chemical transformations in which an acyl group (R–CO–) is transferred from a donor molecule to an acceptor, mediated by an acyltransferase enzyme. These enzymes are classified within the EC 2.3 family, which includes a wide range of transferases that move acyl groups between donors such as acyl-CoA, acyl anhydrides, or other acyl donors, and acceptors such as alcohols, amines, thiols, or sugars. The reaction typically yields esters, amides, or thioesters, depending on the nature of the acceptor.

Acyltransferases exhibit substantial substrate diversity and specificity. Some enzymes use acyl-CoA thioesters as donors and catalyze transfer to oxygen, nitrogen, or sulfur nucleophiles, producing O-, N-, or S-acyl products. Others can transfer acyl groups from alternative donors, including anhydrides or enzyme-bound acyl intermediates. Mechanistic strategies vary, ranging from ping-pong (double-displacement) to sequential Bi-Bi mechanisms, and in some cases involve transient acyl-enzyme intermediates.

Biological roles are broad. Acyltransferases participate in lipid biosynthesis and remodeling (for example, glycerolipid and phospholipid formation), protein and lipid post-translational modifications (such as N- and O-acylation), and detoxification or xenobiotic metabolism through acylation. They also support biotechnological applications, including the enzymatic synthesis of esters and amides, and the engineering of metabolic pathways for the production of specialty lipids and bioactive compounds.

Representative examples include acyl-CoA:cholesterol acyltransferases, which form cholesterol esters; diacylglycerol acyltransferases, which contribute to triglyceride synthesis; and various lysophospholipid acyltransferases involved in phospholipid remodeling.