17beta-HSD5, 3-alpha hydroxysteroid dehydrogenase type 3, 3-alpha-HSD type 2, 3-alpha-HSD1, 3-alpha-hydroxysteroid dehydrogenase type 2, 3-alpha-hydroxysteroid dehydrogenase type I, 3alpha-HSD, 3alpha-HSD type III, 3alpha-HSD/CR, 3alpha-HSD3, 3alpha-HSOR, 3alpha-hydroxysteroid dehydrogenase, 3alpha-hydroxysteroid dehydrogenase type 3, 3alpha-hydroxysteroid dehydrogenase type III, 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase, 3alpha-hydroxysteroid oxidoreductase, AKR1C1, AKR1C14, AKR1C2, AKR1C3, AKR1C33, AKR1C4, AKR1C9, aldo-keto reductase family 1 member C1, aldo-keto reductase family 1 member C2, aldo-keto reductase family 1 member C3, bile acid binding protein, chlordecone reductase, DD2, DD4, dihydrodiol dehydrogenase, dihydrodiol dehydrogenase 4, dihydrodiol/3alpha-hydroxysteroid dehydrogenase, HSD 28, HSD 29, hsdA, More, NADPH-dependent AKR1C9, Naloxone reductase 2, Ps3alphaHSD, type 1 3alpha-HSD, type 3 3alpha-hydroxysteroid dehydrogenase, type 5 17beta-hydroxysteroid dehydrogenase, type I 3alpha-HSD, type III 3-alpha-hydroxysteroid dehydrogenase
hydroxychlor (HPTE), competitive without cofactor but mixed-type inhibition with cofactor, methoxychlor and its metabolite HPTE inhibit rat neurosteroidogenic 3alpha-hydroxysteroid dehydrogenase
about 90% inhibition at 0.1 mM, inhibition kinetics. Apigenin inhibits AKR1C9 in a mixed-type inhibitory mode when the cofactor is used. This indicates that apigenin also affects the cofactor-binding site besides its binding to the active site of the steroid substrate. Docking analysis of the binding of apigenin to rat AKR1C9 with bound NADPH and substrate dihydrotestsosterone
MXC, methoxychlor and its metabolite hydroxychlor (HPTE) inhibit rat neurosteroidogenic 3alpha-hydroxysteroid dehydrogenase. Methoxychlor is primarily used as an insecticide, and it is widely present in the environment
crystal structures of complexes of 17beta-HSD5 with structurally diverse inhibitors derived from high-throughput inhibitor screening, overview. Analysis of interactions between 17beta-HSD5 and inhibitors at the atomic level which enable structure-based drug design for anti-CRPC therapy
binding mode determination of methoxychlor (MXC) and HPTE from the crystal structure of AKR1C14 by molecular docking. HPTE has a higher affinity with the enzyme than methoxychlor. HPTE is more potent than methoxychlor to inhibit both AKR1C14 and retinol dehydrogenase 2 (RDH2, EC 1.1.1.53). Both MXC and HPTE interact with Y55, K84, H117, W227, and Y310 of the enzyme. HPTE also forms hydrogen bond with V25 residue of AKR1C14. Both MXC and HPTE inhibit rat AKR1C14 in a competitive mode against DHT. No inhibition by DMSO