Cinnamoyl-CoA reductase (EC 1.2.1.44), systematically named cinnamaldehyde:NADP+ oxidoreductase (CoA-cinnamoylating) but commonly referred to by the acronym CCR, is an enzyme that catalyzes the reduction of a substituted cinnamoyl-CoA to its corresponding cinnamaldehyde, utilizing NADPH and H+ and releasing free CoA and NADP+ in the process.[1] Common biologically relevant cinnamoyl-CoA substrates for CCR include p-coumaroyl-CoA and feruloyl-CoA, which are converted into p-coumaraldehyde and coniferaldehyde, respectively,[2] though most CCRs show activity toward a variety of other substituted cinnamoyl-CoA's as well.[1] Catalyzing the first committed step in monolignol biosynthesis,[3] this enzyme plays a critical role in lignin formation, a process important in plants both for structural development and defense response.[2]
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