Aldo-keto reductase
From Proteopedia
(Difference between revisions)
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*'''AKR4C14''' involved in detoxification of methylglyoxal and MDA <ref>PMID:32355043</ref>.<br /> | *'''AKR4C14''' involved in detoxification of methylglyoxal and MDA <ref>PMID:32355043</ref>.<br /> | ||
*'''AKR4C17''' involved in glyphosate herbicide resistance <ref>PMID:35739721</ref>.<br /> | *'''AKR4C17''' involved in glyphosate herbicide resistance <ref>PMID:35739721</ref>.<br /> | ||
| - | *'''AKR7A1''' | + | *'''AKR7A1''' and '''AKR7A5''' metabolize the environmental carcinogen aflatoxin B(1) <ref>PMID:12727802</ref>.<br /> |
== Disease == | == Disease == | ||
Mutations in AKR1D1 cause a form of bile acid deficiency which can be fatal in newborns<ref>PMID:20522910</ref>. AKR1D1 inhibitor [[Finasteride]] is used as treatment for benign prostate hyperplasia. | Mutations in AKR1D1 cause a form of bile acid deficiency which can be fatal in newborns<ref>PMID:20522910</ref>. AKR1D1 inhibitor [[Finasteride]] is used as treatment for benign prostate hyperplasia. | ||
Revision as of 09:25, 22 May 2024
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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
- ↑ Brožič P, Turk S, Rižner TL, Gobec S. Inhibitors of aldo-keto reductases AKR1C1-AKR1C4. Curr Med Chem. 2011;18(17):2554-65. PMID:21568892 doi:10.2174/092986711795933713
- ↑ . PMID:110526179
- ↑ Yamamoto K, Wilson DK. Identification, characterization, and crystal structure of an aldo-keto reductase (AKR2E4) from the silkworm Bombyx mori. Arch Biochem Biophys. 2013 Oct 15;538(2):156-63. doi: 10.1016/j.abb.2013.08.018. , Epub 2013 Sep 6. PMID:24012638 doi:http://dx.doi.org/10.1016/j.abb.2013.08.018
- ↑ Saito R, Shimakawa G, Nishi A, Iwamoto T, Sakamoto K, Yamamoto H, Amako K, Makino A, Miyake C. Functional analysis of the AKR4C subfamily of Arabidopsis thaliana: model structures, substrate specificity, acrolein toxicity, and responses to light and [CO(2)]. Biosci Biotechnol Biochem. 2013;77(10):2038-45. PMID:24096666 doi:10.1271/bbb.130353
- ↑ Songsiriritthigul C, Narawongsanont R, Tantitadapitak C, Guan HH, Chen CJ. Structure-function study of AKR4C14, an aldo-keto reductase from Thai jasmine rice (Oryza sativa L. ssp. indica cv. KDML105). Acta Crystallogr D Struct Biol. 2020 May 1;76(Pt 5):472-483. doi:, 10.1107/S2059798320004313. Epub 2020 Apr 23. PMID:32355043 doi:http://dx.doi.org/10.1107/S2059798320004313
- ↑ Li H, Yang Y, Hu Y, Chen CC, Huang JW, Min J, Dai L, Guo RT. Structural analysis and engineering of aldo-keto reductase from glyphosate-resistant Echinochloa colona. J Hazard Mater. 2022 Aug 15;436:129191. PMID:35739721 doi:10.1016/j.jhazmat.2022.129191
- ↑ Ellis EM, Slattery CM, Hayes JD. Characterization of the rat aflatoxin B1 aldehyde reductase gene, AKR7A1. Structure and chromosomal localization of AKR7A1 as well as identification of antioxidant response elements in the gene promoter. Carcinogenesis. 2003 Apr;24(4):727-37. PMID:12727802 doi:10.1093/carcin/bgg016
- ↑ 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
