Caffeic acid 3-O-methyltransferase (COMT) (COMT)

Caffeic acid 3-O-methyltransferase (COMT) is a key enzyme in the phenylpropanoid pathway, primarily responsible for the biosynthesis of lignin in plants. It catalyzes the O-methylation of caffeic acid and 5-hydroxyferulic acid to produce ferulic acid and sinapic acid, respectively, using S-adenosyl-L-methionine as the methyl donor (UniProt: P46484). This enzymatic activity is essential for the production of syringyl (S) lignin subunits, which provide structural integrity and mechanical strength to plant cell walls (PubMed: 20566714). While COMT is not a therapeutic target for human diseases, it is a major target in agricultural biotechnology and the biofuel industry. Genetic modulation of COMT is used to reduce lignin content or alter its composition to improve the processing efficiency of biomass for biofuels and enhance the nutritional quality of forage crops (ScienceDirect: S0960-8524(11)00344-1). Potential challenges in targeting COMT include unintended effects on plant growth, such as increased susceptibility to lodging or altered resistance to environmental stressors. Research into COMT inhibitors is primarily focused on understanding plant metabolism and optimizing biomass for industrial applications.

Other names

Caffeate O-methyltransferase5-hydroxyferulic acid O-methyltransferaseCaffeic acid 3-O-methyltransferaseS-adenosyl-L-methionine:caffeic acid 3-O-methyltransferase

Catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to the 3-hydroxyl group of caffeic acid or the 5-hydroxyl group of 5-hydroxyferulic acid.