RRC ID 33332
著者 Hirade Y, Kotoku N, Terasaka K, Saijo-Hamano Y, Fukumoto A, Mizukami H.
タイトル Identification and functional analysis of 2-hydroxyflavanone C-glucosyltransferase in soybean (Glycine max).
ジャーナル FEBS Lett
Abstract 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.
巻・号 589(15)
ページ 1778-86
公開日 2015-7-8
DOI 10.1016/j.febslet.2015.05.010
PII S0014-5793(15)00363-4
PMID 25979175
MeSH Amino Acid Sequence Catalysis Catalytic Domain Chromatography, High Pressure Liquid Glucosyltransferases / chemistry Glucosyltransferases / classification Glucosyltransferases / metabolism* Mass Spectrometry Molecular Sequence Data Phylogeny Recombinant Proteins / chemistry Recombinant Proteins / metabolism Sequence Homology, Amino Acid Soybeans / enzymology*
IF 3.057
引用数 29
WOS 分野 BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY CELL BIOLOGY
リソース情報
ミヤコグサ・ダイズ GMFL02-51-N04