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Results 1 - 10 of 32 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.357physiological function 3-alpha hydroxysteroid dehydrogenase type 3 has an essential role in the inactivation of 5alpha-dihydrotestosterone preventing binding and activation of androgen receptor from overflowing androgen 743179
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.357evolution 3alpha-HSOR is a member of the aldo-keto reductase superfamily 763094
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.357physiological function 3alpha-hydroxysteroid dehydrogenase catalyzes the oxidation of the 3-hydroxyl group of steroids. The enzymatic conversion is a critical step in the enzymatic assay of urinary sulfated bile acids 743736
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.357metabolism 3alpha-hydroxysteroid dehydrogenase isoform AKR1C4 plays a significant role in bile acid biosynthesis, steroid hormone metabolism, and xenobiotic metabolism 689076
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.357physiological function 3alpha-hydroxysteroid dehydrogenase type 3 plays an essential role in the inactivation of the most potent androgen 5alpha-dihydrotestosterone 740017
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.357more AKR1C14 has two substrate binding sites, the steroid binding and the cofactor binding site 763517
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.357more AKR1C9 has two substrate binding sites, the steroid binding site and the cofactor binding site 762009
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.357more catalytic tetrad N86-S114-Y155-K159, catalytic roles of P185 and T188 and substrate-binding loop flexibility in 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase. Structurally the substrate-binding loop of the residues, T188-K208, is unresolved, while binding with NAD+ causes the appearance of T188-P191 in the binary complex, functional roles of the flexible substrate-binding loop in conformational changes and enzyme catalysis, overview. Simulated molecular modeling gives results that are consistent with the conformational change in the substrate-binding loop after NAD+ binding. These results indicate that P185, T188 and the flexible substrate-binding loop are involved in binding with the nucleotide cofactor and with androsterone and are also involved in catalysis. Homology structure modeling, overview 743632
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.357malfunction downregulation of 3alpha-HSD3 decreases MCF-7 breast cancer cell growth 740017
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.357evolution enzyme 3alpha-HSD/CR belongs to the short chain dehydrogenase/ reductase (SDR) superfamily 742260, 743632
Results 1 - 10 of 32 > >>