Pinus taeda phenylpropenal double-bond reductase: Purification, cDNA cloning, heterologous expression in Escherichia coli, and subcellular localization in P. taeda

A phenylpropenal double-bond reductase (PPDBR) was obtained from cell suspension cultures of loblolly pine (Pinus taeda L.). Its cDNA was subsequently cloned, with the functional recombinant protein expressed in Escherichia coli and characterized. PPDBR readily converted both dehydrodiconiferyl and coniferyl aldehydes into dihydrodehydrodiconiferyl and dihydroconiferyl aldehydes, when NADPH was added as cofactor.