Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase.

@article{Thoden2000CrystallographicEF,
  title={Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase.},
  author={James B. Thoden and T. M. Wohlers and Judith L Fridovich-Keil and Hazel M Holden},
  journal={Biochemistry},
  year={2000},
  volume={39 19},
  pages={5691-701}
}
UDP-galactose 4-epimerase catalyzes the interconversion of UDP-glucose and UDP-galactose during normal galactose metabolism. In humans, deficiencies in this enzyme lead to the complex disorder referred to as epimerase-deficiency galactosemia. Here, we describe the high-resolution X-ray crystallographic structures of human epimerase in the resting state (i.e., with bound NAD(+)) and in a ternary complex with bound NADH and UDP-glucose. Those amino acid side chains responsible for anchoring the… CONTINUE READING

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