Crystal structure of α-glucosyl transfer enzyme XgtA from Xanthomonas campestris WU-9701

Risa Watanabe, Yasuhiro Arimura, Yoshitaka Ishii, Kohtaro Kirimura

研究成果: Article

抜粋

The α-glucosyl transfer enzyme XgtA is a novel type α-Glucosidase (EC 3.2.1.20) produced by Xanthomonas campestris WU-9701. One of the unique properties of XgtA is that it shows extremely high α-glucosylation activity toward alcoholic and phenolic –OH groups in compounds using maltose as an α-glucosyl donor and allows for the synthesis of various useful α-glucosides with high yields. XgtA shows no hydrolytic activity toward sucrose and no α-glucosylation activity toward saccharides to produce oligosaccharides. In this report, the crystal structure of XgtA was solved at 1.72 Å resolution. The crystal belonged to space group P22121, with unit-cell parameters a = 73.07, b = 83.48, and c = 180.79 Å. The β→α loop 4 of XgtA, which is proximal to the catalytic center, formed a unique structure that is not observed in XgtA homologs. Furthermore, XgtA was found to contain unique amino acid residues around its catalytic center. The unique structure of XgtA provides an insight into the mechanism for the regulation of substrate specificity in this enzyme.

元の言語English
ページ(範囲)580-585
ページ数6
ジャーナルBiochemical and Biophysical Research Communications
526
発行部数3
DOI
出版物ステータスPublished - 2020 6 4

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

フィンガープリント Crystal structure of α-glucosyl transfer enzyme XgtA from Xanthomonas campestris WU-9701' の研究トピックを掘り下げます。これらはともに一意のフィンガープリントを構成します。

  • これを引用