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. Rondeau and F. T{\^e}te-Favier and A. Podjarny and J. Reymann and P. Barth and J. Biellmann and D. 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… CONTINUE READING
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References
SHOWING 1-10 OF 28 REFERENCES
The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases.
- Biology, Medicine
- The Journal of biological chemistry
- 1989
- 357
- PDF
Sequence analysis of bovine lens aldose reductase.
- Medicine, Biology
- The Journal of biological chemistry
- 1990
- 51
Kinetic and structural effects of activation of bovine kidney aldose reductase.
- Chemistry, Medicine
- Biochemistry
- 1989
- 52
Bovine lens aldose reductase: tight binding of the pyridine coenzyme.
- Chemistry, Medicine
- Archives of biochemistry and biophysics
- 1990
- 34
Spinach glycolate oxidase and yeast flavocytochrome b2 are structurally homologous and evolutionarily related enzymes with distinctly different function and flavin mononucleotide binding.
- Medicine, Chemistry
- The Journal of biological chemistry
- 1991
- 97
- PDF
Aldose reductase from human skeletal and heart muscle. Interconvertible forms related by thiol-disulfide exchange.
- Medicine, Chemistry
- The Journal of biological chemistry
- 1990
- 60
- PDF
Comparison of the three-dimensional protein and nucleotide structure of the FAD-binding domain of p-hydroxybenzoate hydroxylase with the FAD- as well as NADPH-binding domains of glutathione reductase.
- Chemistry, Medicine
- Journal of molecular biology
- 1983
- 168
Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state.
- Biology, Medicine
- Biochemistry
- 1990
- 212
Isolation and characterization of cloned cDNAs encoding human liver chlordecone reductase.
- Biology, Medicine
- Biochemistry
- 1990
- 71
Production of 2-Keto-L-Gulonate, an Intermediate in L-Ascorbate Synthesis, by a Genetically Modffied Erwinia herbicola
- Biology, Medicine
- Science
- 1985
- 152