Identification of a hydroxycinnamoyl-CoA double bond reductase (HDR) affirms multiple pathways for dihydrochalcone formation in apple.

ABSTRACT: Dihydrochalcones are secondary metabolites with manifold dietary and pharmaceutical properties, but with a yet unclear function in plants. The abundance of dihydrochalcones, particularly phloridzin, makes Malus ssp. unique in the plant kingdom. The gene(s)/enzyme(s) for the key reaction in phloridzin biosynthesis, the reduction in the C3-bridge connecting the aromatic rings A and B of chalcones, have long been searched for. To date, two possible pathways to phloridzin have been described, one via the reduction in p-coumaroyl-CoA and the other via the reduction in naringenin chalcone. In this work, an enzyme from apple leaves, which catalyses the reduction in p-coumaroyl-CoA, was purified and partially sequenced. The newly identified hydroxycinnamoyl-CoA double bond reductase (HDR) has not

SUBMITTER: Schropfer S 

PROVIDER: S-EPMC12483985 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature