Novel NADPH-binding domain revealed by the crystal structure of aldose reductase

@article{Rondeau1992NovelND,
  title={Novel NADPH-binding domain revealed by the crystal structure of aldose reductase},
  author={J. M. Rondeau and Fr{\'e}d{\'e}rique T{\^e}te-Favier and Alberto D. Podjarny and Jean Michel Reymann and Patrick Barth and Jean François Biellmann and Dino Moras},
  journal={Nature},
  year={1992},
  volume={355},
  pages={469-472}
}
ALDOSE reductase is the first enzyme in the polyol pathway and catalyses the NADPH-dependent reduction of D-glucose to D-sorbitol. Under normal physiological conditions aldose reductase participates in osmoregulation1, but under hyperglycaemic conditions it contributes to the onset and development of severe complications in diabetes2. Here we present the crystal structure of pig lens aldose reductase refined to an R-factor of 0.232 at 2.5-Å resolution. It exhibits a single domain folded in an… Expand
The crystal structure of the aldose reductase.NADPH binary complex.
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The crystal structure revealed that the enzyme is a beta/alpha-barrel with the coenzyme-binding domain located at the carboxyl-terminal end of the parallel strands of the barrel, and NADPH is bound to aldose reductase in an unusual manner, more similar to FAD- rather than NAD(P)-dependent oxidoreductases. Expand
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