EC Number |
General Information |
Reference |
---|
1.1.1.357 | physiological 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 |
1.1.1.357 | evolution |
3alpha-HSOR is a member of the aldo-keto reductase superfamily |
763094 |
1.1.1.357 | physiological 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 |
1.1.1.357 | metabolism |
3alpha-hydroxysteroid dehydrogenase isoform AKR1C4 plays a significant role in bile acid biosynthesis, steroid hormone metabolism, and xenobiotic metabolism |
689076 |
1.1.1.357 | physiological function |
3alpha-hydroxysteroid dehydrogenase type 3 plays an essential role in the inactivation of the most potent androgen 5alpha-dihydrotestosterone |
740017 |
1.1.1.357 | more |
AKR1C14 has two substrate binding sites, the steroid binding and the cofactor binding site |
763517 |
1.1.1.357 | more |
AKR1C9 has two substrate binding sites, the steroid binding site and the cofactor binding site |
762009 |
1.1.1.357 | more |
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 |
1.1.1.357 | malfunction |
downregulation of 3alpha-HSD3 decreases MCF-7 breast cancer cell growth |
740017 |
1.1.1.357 | evolution |
enzyme 3alpha-HSD/CR belongs to the short chain dehydrogenase/ reductase (SDR) superfamily |
742260, 743632 |