원문정보
초록
영어
Single vessel multi-enzyme UDP-α-D-glucose recycling system was coupled with a forward glucosylation reaction to produce glucose moiety conjugated novel derivatives of different tetracycline antibiotic analogues. Among five tetracycline analogues used for the reaction, four molecules (chlorotetracycline, doxytetracycline, meclotetracycline, and minotetracycline) were accepted by a glycosyltransferase enzyme, YjiC, from Bacillus licheniformis to produce glucoside derivatives. However, the enzyme was unable to conjugate sugar unit to rolitetracycline. All glucosides of tetracycline derivatives were characterized by ultraviolet absorbance maxima, ultra-pressure liquid chromatography coupled with photo-diode-array, and high-resolution quadruple time-of-flight electrospray mass spectrometry analyses. These synthesized glucosides are novel tetracycline derivatives. The conversion of tetracycline analogues to respective glucosides has been found to be very low yet. This gives the clue that the enzyme has low preferences toward tetracycline molecules. Attachment of bulky group in rolitetracycline might have prevented the molecule to reach the catalytic cleft of GT enzyme. Results of this research could become a basis to explore the possibility of synthesizing glucosylated derivatives of different tetracyclines using GT enzyme.