Abstract
A number of 3β-hydroxy steroids including sterols and some steroid sapogenins can be glucosylated, with UDP-glucose (UDPG) as the sugar source, by lipid-depleted enzyme preparations (‘acetone powders’) obtained from shoots of two to three-week-old Asparagus officinalis plants. Difrerent subcellular localizations of glucosyltransferase activities with various steroid acceptors and different sensitivities of individual reactions to a non-ionic detergent Triton X-100 indicate that at least two UDPG-dependent glucosyltransferases acting on steroids which exhibit entirely different specificity patterns are present in A. officinalis. Particulate fractions contain an enzyme which effectively glucosylates sterols and which is highly stimulated by Triton X-100. This glucosyltransferase seems to be similar to the well-known UDPG: sterol glucosyltransferase isolated earlier from several other higher plants. Another glucosyltransferase present in A. officinalis occurs in a soluble form and is distinctly inhibited by Triton X-100. This enzyme has little activity with sterols but efficiently glucosylates some spirostanol sapogenins. The best substrates are 5β-spirostanols: sarsasapogenin (the aglycone of steroid saponins present in A. officinalis) and its 25-epimer, smilagenin.
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