Aldo-keto reductase

spinqualitylabelsall models Human AKR1B10 complex with polyfluorinated inhibitor and NADP 4icc Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D SEE ALSO: Hydroxysteroid dehydrogenase Function Aldo-keto reductase (AKR) is a protein family which contains enzymes that reduce carbonyl substrates like sugar aldehyde, keto-steroid, keto-prostaglandin, retinal, quinones and lipid peroxidation by-products to primary alcohol. AKR uses NADP as a cofactor. AKRs contain a conserved catalytic tetrad consisting of Tyr, Asp, Lys and His. AKR1B10 reduces aliphatic and aromatic aldehydes. It is expressed in adrenal gland, small intestines and colon. AKR1B14 is involved in synthesis of prostaglandin F and detoxification of products of lipid peroxidation. AKR1C4 interconverts steroidal hormone between its active and inactive form. AKR1C13 involved in detoxification of xenobiotics in the stomach. AKR1D1 is responsible for the catalysis of 5-β-reduction of bile acid intermediates and steroid hormones carrying a δ(4)-3-one structure. AKR2E4 is involved in regulation of the molting hormone ecdysone. AKR4C8 and AKR4C9 detoxify sugar-derived reactive carbonyls. AKR4C14 involved in detoxification of methylglyoxal and MDA . AKR4C17 involved in glyphosate herbicide resistance . AKR7A1 and AKR7A5 metabolize the environmental carcinogen aflatoxin B(1) . AKR11C1 uses substrates with a long aliphatic tails . AKR14A1 involved in metabolism of methylglyoxal . Disease Mutations in AKR1D1 cause a form of bile acid deficiency which can be fatal in newborns. AKR1D1 inhibitor Finasteride is used as treatment for benign prostate hyperplasia. Structural highlights The active site of AKR1B10 contains the cofactor NADP and a polyfluorinated inhibitor. Water molecules are shown as red spheres. Tyr and His are part of the enzyme catalytic tetrad. NADP and polyfluorinated inhibitor are situated in the tunnel. 3D structures of aldo-keto reductase Aldo-keto reductase 3D structures

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