Structural highlights
FunctionPublication Abstract from PubMedThe alpha-glucosyl transfer enzyme XgtA is a novel type alpha-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 alpha-glucosylation activity toward alcoholic and phenolic -OH groups in compounds using maltose as an alpha-glucosyl donor and allows for the synthesis of various useful alpha-glucosides with high yields. XgtA shows no hydrolytic activity toward sucrose and no alpha-glucosylation activity toward saccharides to produce oligosaccharides. In this report, the crystal structure of XgtA was solved at 1.72 A resolution. The crystal belonged to space group P22121, with unit-cell parameters a = 73.07, b = 83.48, and c = 180.79 A. The beta-->alpha 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. Crystal structure of alpha-glucosyl transfer enzyme XgtA from Xanthomonas campestris WU-9701.,Watanabe R, Arimura Y, Ishii Y, Kirimura K Biochem Biophys Res Commun. 2020 Jun 4;526(3):580-585. doi:, 10.1016/j.bbrc.2020.03.109. Epub 2020 Apr 1. PMID:32247611[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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