Aldo-keto reductase
From Proteopedia
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<StructureSection load='4icc' size='350' side='right' caption='Human AKR1B10 complex with polyfluorinated inhibitor and NADP [[4icc]]' scene='49/491879/Cv/1' > | <StructureSection load='4icc' size='350' side='right' caption='Human AKR1B10 complex with polyfluorinated inhibitor and NADP [[4icc]]' scene='49/491879/Cv/1' > | ||
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== Function == | == 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<ref>PMID:25304492</ref>. AKR uses NADP as a cofactor. AKRs contain a conserved catalytic tetrad consisting of Tyr, Asp, Lys and His. | 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<ref>PMID:25304492</ref>. AKR uses NADP as a cofactor. AKRs contain a conserved catalytic tetrad consisting of Tyr, Asp, Lys and His. | ||
Revision as of 07:40, 29 December 2016
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3D structures of aldo-keto reductase
Updated on 29-December-2016
References
- ↑ Penning TM. The aldo-keto reductases (AKRs): Overview. Chem Biol Interact. 2015 Jun 5;234:236-46. doi: 10.1016/j.cbi.2014.09.024. Epub, 2014 Oct 7. PMID:25304492 doi:http://dx.doi.org/10.1016/j.cbi.2014.09.024
- ↑ Drury JE, Mindnich R, Penning TM. Characterization of disease-related 5beta-reductase (AKR1D1) mutations reveals their potential to cause bile acid deficiency. J Biol Chem. 2010 Aug 6;285(32):24529-37. doi: 10.1074/jbc.M110.127779. Epub 2010, Jun 3. PMID:20522910 doi:http://dx.doi.org/10.1074/jbc.M110.127779
- ↑ Cousido-Siah A, Ruiz FX, Mitschler A, Porte S, de Lera AR, Martin MJ, Manzanaro S, de la Fuente JA, Terwesten F, Betz M, Klebe G, Farres J, Pares X, Podjarny A. Identification of a novel polyfluorinated compound as a lead to inhibit the human enzymes aldose reductase and AKR1B10: structure determination of both ternary complexes and implications for drug design. Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):889-903. doi:, 10.1107/S1399004713033452. Epub 2014 Feb 27. PMID:24598757 doi:http://dx.doi.org/10.1107/S1399004713033452
