Planta Med 1985; 51(2): 104-107
DOI: 10.1055/s-2007-969419
Research Articles

© Georg Thieme Verlag Stuttgart · New York

Partial Purification and Characterization of UDP-Glucose: Salicyl Alcohol Glucosyltransferase from Gardenia jasminoides Cell Cultures

H. Mizukami, T. Terao, H. Ohashi
  • Faculty of Pharmaceutical Sciences, Nagasaki University, Bunkyomachi 1-14, Nagasaki 852, Japan
Further Information

Publication History



Publication Date:
26 February 2007 (online)


A new enzyme, UDP-glucose: salicyl alcohol glucosyltransferase, was purified 110-fold from Gardenia jasminoides cell cultures. The enzyme catalyzes position-specific glucosylation of salicyl alcohol to form salicin using UDP-glucose as a glucose donor. The molecular weight of the enzyme as estimated by gel filtration is 51,000. Apparent Km values for salicyl alcohol and UDP-glucose are 0.11 and 0.031 mM, respectively. The enzyme shows a pH optimum between 9.0 and 9.5. Sulfhydryl inhibitors and some divalent cations inhibit the enzyme activity. The glucosyltransferase exhibits a strict substrate specificity for salicyl alcohol.