Related Experiment Video
Updated: Aug 9, 2026
Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
Published on: May 23, 2025
Purification, crystallization and preliminary X-ray diffraction studies of N-acetylglucosamine-phosphate mutase from
Yuichi Nishitani1, Daisuke Maruyama, Tsuyoshi Nonaka
1Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Abstract:
N-acetylglucosamine-phosphate mutase (AGM1) is an essential enzyme in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc) in eukaryotes and belongs to the alpha-D-phosphohexomutase superfamily. AGM1 from Candida albicans (CaAGM1) was purified and crystallized by the sitting-drop vapour-diffusion method. The crystals obtained belong to the primitive monoclinic space group P2(1), with unit-cell parameters a = 60.2, b = 130.2, c = 78.0 angstroms, beta = 106.7 degrees. The crystals diffract X-rays to beyond 1.8 angstroms resolution using synchrotron radiation.
