LPL operates through a serine hydrolase mechanism. The enzyme has a catalytic triad composed of serine, histidine, and aspartate residues. The catalytic process begins when the serine residue attacks the ester bond of the triglyceride, forming a covalent acyl-enzyme intermediate. This intermediate is then hydrolyzed, releasing the free fatty acids and glycerol. The precise arrangement of these residues in the active site is crucial for the enzyme's catalytic activity.
