Gallotannin biosynthesis: two new galloyltransferases from Rhus typhina leaves preferentially acylating hexa- and heptagalloylglucoses.

Current enzyme studies on the biosynthesis of gallotannins with cell-free extracts from leaves of staghorn sumac (Rhus typhina L.) revealed the existence of two new beta-glucogallin-dependent galloyltransferases (EC 2.3.1.-) that preferentially catalyzed the acylation of hexa- and heptagalloylglucoses. One enzyme was most active with the hexagalloylglucose, 3-O-digalloyl-1,2,4,6-tetra-O-galloylglucose, to form the corresponding heptagalloylglucose, 3-O-trigalloyl-1,2,4,6-tetra-O-galloylglucose. This polyester, in turn, was the preferred substrate for a second enzyme that catalyzed its conversion to higher substituted derivatives. This latter enzyme also displayed considerable affinity towards 2-O-digalloyl-1,3,4,6-tetra-O-galloylglucose which was acylated to various hepta- and octagalloylglucoses. These recent findings, together with data from earlier reported related enzymes, allowed the presentation of a scheme that summarizes the major transitions in the biogenetic routes from 1,2,3,4,6-pentagalloylglucose to complex gallotannins.