UGT88B2: A promiscuous O-glycosyltransferase from Carthamus tinctorius |
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Authors: | Song-yang Sui Rui-mingqian Guo Ke-bo Xie Lin Yanga |
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Institution: | 1. College of Life and Environmental Sciences, Minzu University of China, Beijing 100081, China;2. State Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing 100050, China |
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Abstract: | Objective: In order to obtain new glycosyltransferases with highly efficient catalysis, the glycosyltransferases from Carthamus tinctorius which contains diverse types of glycosides were mined. Methods: A new glycosyltransferase gene (UGT88B2) with full length was obtained by PCR and further transformed into Escherichia coli for heterologous expression. The catalytic activity of recombinant UGT88B2 was determined by HPLC-MSn. The structures of representative catalytic products were elucidated by MS and NMR.
Results: UGT88B2 exhibited catalytic promiscuity and various patterns in glycosylation of flavonoids with high efficiency.
Conclusion: A new glycosyltransferase named UGT88B2 was successfully mined and can be employed as enzymatic tools in glycosylation of flavonoids. |
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Keywords: | Carthamus tinctorius L enzyme promiscuity glycosyltransferase O-glycosides |
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