CommentaryXenobiotic carbonyl reduction and physiological steroid oxidoreduction: The pluripotency of several hydroxysteroid dehydrogenases
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Carbonyl reductase sniffer from the model organism daphnia: Cloning, substrate determination and inhibitory sensitivity
2019, Chemico-Biological InteractionsCitation Excerpt :However, endosulfan (an off-patent organochlorine insecticide and acaricide that is being phased out globally) potently inhibited both sniffer enzymes with Ki-values of 9.2 μM (sniffer from D. magna) and 12.0 μM (sniffer from D. pulex) (Fig. 4). Human carbonyl reductase 1 (CBR1) is an important reductase in the metabolism of xenobiotic carbonyl compounds [16,18,19,33–35] and, in addition, plays a role in the protection against lipid peroxidation derived reactive aldehydes [13,17]. Thus, this enzyme is of high interest as a defense mechanism against oxidative stress and, in more detail, “carbonyl stress” [30].
Virtual screening applications in short-chain dehydrogenase/reductase research
2017, Journal of Steroid Biochemistry and Molecular BiologyEffect of defined green tea extract in various dosage schemes on drug-metabolizing enzymes in mice in vivo
2014, Journal of Functional Foods17β-Hydroxysteroid dehydrogenases (17β-HSDs) as therapeutic targets: Protein structures, functions, and recent progress in inhibitor development
2011, Journal of Steroid Biochemistry and Molecular BiologyCitation Excerpt :As their names imply, they regio- and stereo-selectively catalyze the oxidoreduction in different positions of steroidal substrates (3α-, 3β-, 11β-, 17β-, 20α- and 20β-position). The steroid-converting HSDs play central roles in the biosynthesis and inactivation of steroid hormones, but some of them are also involved in the metabolism of diverse non-steroidal compounds [1–3]. In the classical view, hormones are synthesized and excreted by endocrine glands and act on target cells or target tissues via a receptor mechanism after being transported by the circulatory system (“endocrinology”).