Crystal structure of S-adenosylhomocysteine hydrolase from rat liver.

@article{Hu1999CrystalSO,
  title={Crystal structure of S-adenosylhomocysteine hydrolase from rat liver.},
  author={Yongbo Hu and Junichi Komoto and Yafei Huang and Tomoharu Gomi and Hirofumi Ogawa and Yoshimi Takata and Motoji Fujioka and Fusao Takusagawa},
  journal={Biochemistry},
  year={1999},
  volume={38 26},
  pages={8323-33}
}
The crystal structure of rat liver S-adenosyl-L-homocysteine hydrolase (AdoHcyase, EC 3.3.1.1) which catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) has been determined at 2.8 A resolution. AdoHcyase from rat liver is a tetrameric enzyme with 431 amino acid residues in each identical subunit. The subunit is composed of the catalytic domain, the NAD+-binding domain, and the small C-terminal domain. Both catalytic and NAD+-binding domains are folded into an ellipsoid with a… CONTINUE READING