Crystal structure of rat biliverdin reductase

@article{Kikuchi2001CrystalSO,
  title={Crystal structure of rat biliverdin reductase},
  author={Akihiro Kikuchi and Sam-Yong Park and Hideyuki Miyatake and Danyu Sun and Michihiko Sato and Tadashi Yoshida and Yoshitsugu Shiro},
  journal={Nature Structural Biology},
  year={2001},
  volume={8},
  pages={221-225}
}
Biliverdin reductase (BVR) is a soluble cytoplasmic enzyme that catalyzes the conversion of biliverdin to bilirubin using NADH or NADPH as electron donor. Bilirubin is a significant biological antioxidant, but it is also neurotoxic and the cause of kernicterus. In this study, we have determined the crystal structure of rat BVR at 1.4 Å resolution. The structure contains two domains: an N-terminal domain characteristic of a dinucleotide binding fold (Rossmann fold) and a C-terminal domain that… 
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TLDR
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TLDR
The protein produced by an expression plasmid in which the insert was cloned in frame with lacZ sequences was characterized, and demonstrated dual pH and cofactor dependence, but as suggested by kinetic analysis, the human enzyme may also use NADH as cofactor, as opposed to the rat reductase, which most likely utilizes only NADPH under physiological conditions.
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TLDR
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TLDR
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TLDR
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