From cell suspension cultures ofRauwolfiaserpentinaBenth. a new enzyme activity was isolated and its properties determined. The enzyme is a soluble protein and catalyzes the transfer of a glucose moiety from UDPG to a wide variety of phenolic compounds withp-nitrophenol as one of the best substrates (Km = 1.21 mM, UDPG = 0.54 mM). In contrast to the membrane-bound UDPG: vomilenine-21-OH-β-D-glucosyltransferase fromRauwolfiaserpentinacells, this enzyme is not able to glucosylate indole alkaloids. The enzyme activity has been detected in 14 callus cultures belonging to 10 different plant families.