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査読

9 被引用数 (Scopus)


The α-glucosyl transfer enzyme XgtA is a novel type α-Glucosidase (EC 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.

ジャーナルBiochemical and Biophysical Research Communications
出版ステータスPublished - 2020 6月 4

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学


「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。これらがまとまってユニークなフィンガープリントを構成します。