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Article

Uridine Diphosphate-Dependent Glycosyltransferases from Bacillus subtilis ATCC 6633 Catalyze the 15-O-Glycosylation of Ganoderic Acid A

1
Department of Biological Sciences and Technology, National University of Tainan, Tainan 70005, Taiwan
2
Department of Food Science, National Quemoy University, Kinmen County 892, Taiwan
3
Biodiversity Research Center, Academia Sinica, Taipei 115, Taiwan
4
Department of Biotechnology, Chia Nan University of Pharmacy and Science, No. 60, Sec. 1, Erh-Jen Rd., Jen-Te District, Tainan 71710, Taiwan
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Int. J. Mol. Sci. 2018, 19(11), 3469; https://doi.org/10.3390/ijms19113469
Received: 11 October 2018 / Revised: 30 October 2018 / Accepted: 3 November 2018 / Published: 5 November 2018
(This article belongs to the Special Issue Microbial Enzymes)
Bacillus subtilis ATCC (American type culture collection) 6633 was found to biotransform ganoderic acid A (GAA), which is a major lanostane triterpenoid from the medicinal fungus Ganoderma lucidum. Five glycosyltransferase family 1 (GT1) genes of this bacterium, including two uridine diphosphate-dependent glycosyltransferase (UGT) genes, BsUGT398 and BsUGT489, were cloned and overexpressed in Escherichia coli. Ultra-performance liquid chromatography confirmed the two purified UGT proteins biotransform ganoderic acid A into a metabolite, while the other three purified GT1 proteins cannot biotransform GAA. The optimal enzyme activities of BsUGT398 and BsUGT489 were at pH 8.0 with 10 mM of magnesium or calcium ion. In addition, no candidates showed biotransformation activity toward antcin K, which is a major ergostane triterpenoid from the fruiting bodies of Antrodia cinnamomea. One biotransformed metabolite from each BsUGT enzyme was then isolated with preparative high-performance liquid chromatography. The isolated metabolite from each BsUGT was identified as ganoderic acid A-15-O-β-glucoside by mass and nuclear magnetic resonance spectroscopy. The two BsUGTs in the present study are the first identified enzymes that catalyze the 15-O-glycosylation of triterpenoids. View Full-Text
Keywords: ganoderic acid; Bacillus subtilis; biotransformation; UDP-glycosyltransferase ganoderic acid; Bacillus subtilis; biotransformation; UDP-glycosyltransferase
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MDPI and ACS Style

Chang, T.-S.; Wu, J.-Y.; Wang, T.-Y.; Wu, K.-Y.; Chiang, C.-M. Uridine Diphosphate-Dependent Glycosyltransferases from Bacillus subtilis ATCC 6633 Catalyze the 15-O-Glycosylation of Ganoderic Acid A. Int. J. Mol. Sci. 2018, 19, 3469. https://doi.org/10.3390/ijms19113469

AMA Style

Chang T-S, Wu J-Y, Wang T-Y, Wu K-Y, Chiang C-M. Uridine Diphosphate-Dependent Glycosyltransferases from Bacillus subtilis ATCC 6633 Catalyze the 15-O-Glycosylation of Ganoderic Acid A. International Journal of Molecular Sciences. 2018; 19(11):3469. https://doi.org/10.3390/ijms19113469

Chicago/Turabian Style

Chang, Te-Sheng, Jiumn-Yih Wu, Tzi-Yuan Wang, Kun-Yuan Wu, and Chien-Min Chiang. 2018. "Uridine Diphosphate-Dependent Glycosyltransferases from Bacillus subtilis ATCC 6633 Catalyze the 15-O-Glycosylation of Ganoderic Acid A" International Journal of Molecular Sciences 19, no. 11: 3469. https://doi.org/10.3390/ijms19113469

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