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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ALDR_HUMAN ALDR_HUMAN]] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. | [[http://www.uniprot.org/uniprot/ALDR_HUMAN ALDR_HUMAN]] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. | ||
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== Publication Abstract from PubMed == | |||
The peroxisome proliferator, WY 14,643 exhibits a pure non-competitive inhibition pattern in the aldehyde reduction and in alcohol oxidation activities of human Aldose reductase (hAR). Fluorescence emission measurements of the equilibrium dissociation constants, Kd, of oxidized (hAR*NADP+) and reduced (hAR*NADPH) holoenzyme complexes display a 2-fold difference between them. Kd values for the dissociation of WY 14,643 from the oxidized (hAR*NADP+*WY 14,643) and reduced (hAR*NADPH*WY 14,643) ternary complexes are comparable to each other. The ternary complex structure of hAR*NADP+*WY 14,643 reveals the first structural evidence of a fibrate class drug binding to hAR. These observations demonstrate how fibrate molecules such as WY 14,643, besides being valued as agonists for PPAR, also inhibit hAR. | |||
Characterization of WY 14,643 and its Complex with Aldose Reductase.,Sawaya MR, Verma M, Balendiran V, Rath NP, Cascio D, Balendiran GK Sci Rep. 2016 Oct 10;6:34394. doi: 10.1038/srep34394. PMID:27721416<ref>PMID:27721416</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
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</StructureSection> | </StructureSection> | ||