High-resolution X-ray structure of UDP-galactose 4-epimerase complexed with UDP-phenol.

@article{Thoden1996HighresolutionXS,
  title={High-resolution X-ray structure of UDP-galactose 4-epimerase complexed with UDP-phenol.},
  author={James B. Thoden and Perry Allen Frey and Hazel M Holden},
  journal={Protein science : a publication of the Protein Society},
  year={1996},
  volume={5 11},
  pages={2149-61}
}
UDP-galactose 4-epimerase from Escherichia coli catalyzes the interconversion of UDP-glucose and UDP-galactose. In recent years, the enzyme has been the subject of intensive investigation due in part to its ability to facilitate nonstereospecific hydride transfer between beta-NADH and a 4-keto hexopyranose intermediate. The first molecular model of the epimerase from E. coli was solved to 2.5 A resolution with crystals grown in the presence of a substrate analogue, UDP-phenol (Bauer AJ, Rayment… CONTINUE READING