Metabolic Regulation of Aldo-Keto Reductases

Dear Colleagues,

The aldo-keto reductase (AKR) superfamily includes 14 different families (AKR1 to AKR14), which have more than one hundred members. AKRs are NAD(P)H-dependent oxidoreductases sharing several structural and functional features. With some exceptions, such as the AKR2, AKR6, and AKR7 families, AKRs are monomeric enzymes composed of approximately 320 amino acids. These enzymes are characterized by an (α/β)8-barrel folding motif and exhibit a peculiar cofactor binding site able to promote, upon binding, significant structural rearrangements preceding the substrate binding. The different families exhibit a wide array of substrate specificities that may partially overlap, creating a very intriguing scenario of functions. AKRs catalyze the reduction of aldehydic and ketonic groups belonging to many different molecules, including monosaccharides, ketosteroids, prostaglandins, and aflatoxins. AKRs are also able to catalyze the oxidation of hydroxysteroids, which are trans-dihydro-diols of polycyclic aromatic hydrocarbons, and have been found to be components of potassium channels. AKRs are quite diffuse in nature in terms of protein type, relative abundance, and functions, and are present in prokaryotes and eukaryotes in a species-specific manner. The large amount of attention paid to many mammalian AKRs as potential therapeutic targets for different pathological states with the aim of drug development is indicative of the relevance of this enzyme superfamily. Modulation of AKR activity through both allosteric interactions and protein expression remains an open field of investigation. The aim of this Special Issue is to provide a platform for furthering the topic with the hope of the disclosure of new relationships in the metabolic control of these enzymes.

Prof. Dr. Umberto Mura
Guest Editor

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