Cinnamoyl-CoA reductase (CCR) (CCR)

Cinnamoyl-CoA reductase (CCR) is a key regulatory enzyme in the phenylpropanoid pathway, specifically catalyzing the first committed step in the biosynthesis of monolignols, the precursors of lignin (UniProt P43226). The enzyme facilitates the NADPH-dependent reduction of hydroxycinnamoyl-CoA esters, such as feruloyl-CoA and p-coumaroyl-CoA, into their corresponding cinnamaldehydes (PubMed 9207110). Lignin is a complex phenolic polymer essential for structural support, water transport, and defense against pathogens in vascular plants (PubMed 11573015). While CCR is not a therapeutic target for human disease, it is a major focus in agricultural biotechnology and the bioenergy industry (PubMed 21079108). Modulating CCR activity allows for the engineering of plants with reduced lignin content or altered lignin composition, which significantly improves the efficiency of cellulosic ethanol production and enhances the digestibility of forage crops (PubMed 20435444). However, severe suppression of CCR can lead to "lignin-deficiency syndrome," characterized by stunted growth and impaired vascular development (PubMed 17556505).

Other names

Feruloyl-CoA reductaseCinnamoyl-CoA:NADP+ oxidoreductaseCCR1CCR2

Cinnamoyl-CoA reductase catalyzes the NADPH-dependent reduction of hydroxycinnamoyl-CoA thioesters into their corresponding aldehydes, which is the first committed step in the monolignol biosynthetic pathway (EC 1.2.1.44).