Cinnamyl alcohol dehydrogenase (CAD)

Cinnamyl alcohol dehydrogenase (CAD) is a plant enzyme (EC 1.1.1.195) that catalyzes the final NADPH-dependent reduction of cinnamyl aldehydes to their corresponding alcohols—p-coumaryl, coniferyl, and sinapyl alcohols—which are essential precursors for lignin biosynthesis in plant cell walls. As part of the oxidoreductase (short-chain dehydrogenase/reductase, SDR) family, CAD is found in almost all vascular plants, typically as a multigene family with functionally redundant or tissue-specific isoforms. The enzyme plays a crucial role in determining lignin content and composition, influencing plant structural properties and resistance to pathogens and environmental stresses. While vital for plant physiology, there is currently no evidence supporting its direct relevance or targeting in human therapeutic applications.

Other names

cinnamyl-alcohol:NADP+ oxidoreductasecinnamyl alcohol dehydrogenaseCAD(other gene/protein-specific abbreviations in plants, e.g., AtCAD, OsCAD, HcCAD for species-specific variants)

Enzymatic NADPH-dependent reduction of cinnamyl aldehydes to monolignols (p-coumaryl, coniferyl, and sinapyl alcohols); Genetic inhibition (RNAi, knockouts) leads to altered lignin structure and function in plant studies