Feruloyl coenzyme A synthetase (FCS)

Feruloyl coenzyme A synthetase (EC 6.2.1.34) is an enzyme primarily found in plants and specialized bacteria that catalyzes the conversion of ferulic acid into feruloyl-CoA using ATP and Coenzyme A. In plants, it plays a critical role in the phenylpropanoid pathway, facilitating the biosynthesis of lignin and suberin, which are essential for structural integrity and environmental defense. In certain bacteria, such as Pseudomonas and Streptomyces species, the enzyme is part of the catabolic pathway that degrades lignin-derived aromatic compounds into vanillin, a high-value aromatic compound used extensively in the food and fragrance industries. Although it shares structural homology with human long-chain acyl-CoA synthetases involved in fatty acid metabolism, it is not currently recognized as a therapeutic target for human disease. Its primary applications are found in metabolic engineering and synthetic biology for the sustainable production of aromatic chemicals.

Other names

Ferulate-CoA ligasetrans-feruloyl-CoA synthaseFeruloyl-CoA synthetaseFeruloyl-CoA ligasetrans-ferulate:CoA ligase (ATP-hydrolysing)

The enzyme catalyzes the ATP-dependent activation of ferulic acid into its active thioester form, feruloyl-CoA, which serves as a central intermediate in plant secondary metabolism and bacterial catabolic pathways.