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[1]. 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.
- AKRB14 is involved in sythesis of prostaglandin F and detoxification of products of lipid peroxidation.
- AKR1D1 is responsible for the catalysis of 5-β-reduction of bile acid intermediates and steroid hormones carrying a δ(4)-3-one structure.
Disease
Mutations in AKR1D1 cause a form of bile acid deficiency which can be fatal in newborns[2].
3D structures of aldo-keto reductase
Updated on 28-December-2016
See Hydroxysteroid dehydrogenase 20-alpha HSD
See Hydroxysteroid dehydrogenase 3-alpha HSD
See Prostaglandin F synthase
See Hydroxysteroid dehydrogenase 17-alpha HSD
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