Abstract
Aldose reductase (ALR2) has long been a target for drug design to combat complications which arise in diabetes (Dvornik et al., 1973). The enzyme’s ability to reduce in an NADPH-dependent manner, glucose in its carbonyl-containing, open chain form to sorbitol has been linked to a number of these complications affecting a number of tissues. A large number of ALR2 inhibitors have been developed (reviewed in Sarges & Oates, 1993) but most have not proven to be clinically effective. These disappointing results may be attributed to the inhibition of other members of the aldo-keto reductase family of proteins. This set of enzymes shares considerable sequence homology and consequently has overlapping substrate and inhibitor specificity.
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Wilson, D.K., Nakano, T., Petrash, J.M., Quiocho, F.A. (1996). Structural Studies of Aldo-Keto Reductase Inhibition. In: Weiner, H., Lindahl, R., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 6. Advances in Experimental Medicine and Biology, vol 414. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5871-2_49
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DOI: https://doi.org/10.1007/978-1-4615-5871-2_49
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