標題: Diversity of sugar acceptor of glycosyltransferase 1 from Bacillus cereus and its application for glucoside synthesis
作者: Chiu, Hsi-Ho
Shen, Mo-Yuan
Liu, Yuan-Ting
Fu, Yu-Lieh
Chiu, Yu-An
Chen, Ya-Huei
Huang, Chin-Ping
Li, Yaw-Kuen
應用化學系
Department of Applied Chemistry
關鍵字: Glucosyltransferase;BcGT1;O-glucoside;S-glucoside;N-glucoside
公開日期: May-2016
摘要: Glycosyltransferase 1 from Bacillus cereus (BcGT1) catalyzes the transfer of a glucosyl moiety from uridine diphosphate glucose (UDP-glucose) to various acceptors; it was expressed and characterized. The specificity of acceptors was found to be broad: more than 20 compounds classified into O-, S-, and N-linkage glucosides can be prepared with BcGT1 catalysis. Based on this work, we conclude that the corresponding acceptors of these compounds must possess the following features: (1) the acceptors must contain at least one aromatic or fused-aromatic or heteroaromatic ring; (2) the reactive hydroxyl or sulfhydryl or amino group can attach either on the aromatic ring or on its aliphatic side chain; and (3) the acceptors can be a primary, secondary, or even a tertiary amine. Four representative acceptors-fluorescein methyl ester, 17-beta-estradiol, 7-mercapto-4-methylcoumarin, and 6-benzylaminopurine-were chosen as a candidate acceptor for O-, S-, and N-glucosidation, respectively. These enzymatic products were purified and the structures were confirmed with mass and NMR spectra. As all isolated glucosides are beta-anomers, BcGT1 is confirmed to be an inverting enzyme. This study not only demonstrates the substrate promiscuity of BcGT1 but also showed the great application prospect of this enzyme in bioconversion of valuable bioactive molecules.
URI: http://dx.doi.org/10.1007/s00253-015-7270-1
http://hdl.handle.net/11536/133630
ISSN: 0175-7598
DOI: 10.1007/s00253-015-7270-1
期刊: APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume: 100
Issue: 10
起始頁: 4459
結束頁: 4471
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