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Molecular Modelling Calculations on the Binding of D- and L-Xylose to Wild-Type Aldose Reductase and its H110Q and H110A Mutants

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 372))

Abstract

Human aldose reductase (hAR), an NADPH-dependent enzyme, catalyzes the reversible reduction of a wide variety of carbonyl-containing compounds to their respective alcohol counterparts (Flynn and Green, 1993). Although a physiological role for this enzyme has not yet been established, inhibitors of hAR appear to be effective in the treatment of diabetic neuropathy (Masson and Boulton, 1990).

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References

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© 1995 Springer Science+Business Media New York

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De Winter, H.L., von Itzstein, M. (1995). Molecular Modelling Calculations on the Binding of D- and L-Xylose to Wild-Type Aldose Reductase and its H110Q and H110A Mutants. In: Weiner, H., Holmes, R.S., Wermuth, B. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 5. Advances in Experimental Medicine and Biology, vol 372. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1965-2_28

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  • DOI: https://doi.org/10.1007/978-1-4615-1965-2_28

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-5808-4

  • Online ISBN: 978-1-4615-1965-2

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