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Identification and functional analysis of 2‐hydroxyflavanone C ‐glucosyltransferase in soybean ( Glycine max )
Author(s) -
Hirade Yoshihiro,
Kotoku Naoyuki,
Terasaka Kazuyoshi,
Saijo-Hamano Yumiko,
Fukumoto Akemi,
Mizukami Hajime
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.05.010
Subject(s) - glucosyltransferase , glycine , chemistry , alanine , glucosyltransferases , biochemistry , enzyme , stereochemistry , amino acid
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.