Reference - Detail
| RRC ID | 33332 |
|---|---|
| Author | Hirade Y, Kotoku N, Terasaka K, Saijo-Hamano Y, Fukumoto A, Mizukami H. |
| Title | Identification and functional analysis of 2-hydroxyflavanone C-glucosyltransferase in soybean (Glycine max). |
| Journal | 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. |
| Volume | 589(15) |
| Pages | 1778-86 |
| Published | 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 |
| Times Cited | 29 |
| WOS Category | BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY CELL BIOLOGY |
| Altmetric score |
オルトメトリクス指標項目
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| The most frequently cited source | Patent(IFI CLAIMS) |
| Total number of mentions | 1 |
| Altmetric score changes over past 6months | 0.0 |
| Resource | |
| Lotus / Glycine | GMFL02-51-N04 |