feruloylation

Feruloylation is a post-translational modification where ferulic acid, a phenolic compound, is esterified to specific amino acid residues within proteins. This process primarily occurs on serine and threonine residues, forming a feruloyl ester linkage. Feruloylation is found in a variety of organisms, including plants, bacteria, and fungi. In plants, it is particularly important in cell wall biosynthesis, contributing to the structural integrity and defense mechanisms of plant tissues. The feruloyl groups can cross-link polysaccharides, enhancing the rigidity of the cell wall. In other organisms, feruloylation has been implicated in protein stability, enzyme activity, and interactions with other molecules. The presence and extent of feruloylation can vary depending on the protein, cellular conditions, and environmental stimuli. Enzymes known as feruloyl transferases are responsible for catalyzing this modification. The study of feruloylation is relevant to fields such as plant biology, food science, and biotechnology due to its impact on the properties and functions of biological macromolecules.