期刊
FEBS LETTERS
卷 589, 期 15, 页码 1778-1786出版社
WILEY
DOI: 10.1016/j.febslet.2015.05.010
关键词
2-Hydroxyflavanone C-glucosyltransferase; Enzymatic aryl-C-glucosylation; C-Glucoside biosynthesis; Catalytic residues; Structural modeling; Secondary metabolites
资金
- Graduate School of Frontier Biosciences, Osaka University
- JSPS KAKENHI [25460127]
- Grants-in-Aid for Scientific Research [25460127] Funding Source: KAKEN
C-Glucosyltransferase is an enzyme that mediates carbon-carbon bond formation to generate C-glucoside metabolites. Although it has been identified in several plant species, the catalytic amino acid residues required for C-glucosylation activity remain obscure. Here, we identified a 2-hydroxyflavanone C-glucosyltransferase (UGT708D1) in soybean. We found that three residues, His20, Asp85, and Arg292, of UGT708D1 were located at the predicted active site and evolutionarily conserved. The substitution of Asp85 or Arg292 with alanine destroyed C-glucosyltransferase activity, whereas the substitution of His20 with alanine abolished C-glucosyltransferase activity but enabled O-glucosyltransferase activity. The catalytic mechanism is discussed on the basis of the findings. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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