3α-Hydroxysteroid dehydrogenase is a key enzyme catalyzing steroid metabolism. Its core function is to reversibly catalyze the oxidation of 3α-hydroxysteroids to 3-oxosteroids, using NAD+ or NADP+ as cofactors. As a protein, its molecular weight and optimal reaction conditions vary depending on the source (e.g., human, rat, or bacterial) and subtype. For example, some human subtypes prefer to use NADPH as a cofactor and exhibit optimal activity in a near-neutral environment with a pH of 6.8–7.4. The purified product is typically a white powder.
3α-Hydroxysteroid Dehydrogenase from
Pseudomonas testosterone has been used:
- in the preparation of composite electrode platform to for the determination of androsterone
- in potassium phosphate buffer for the bioluminescent assay of bile acids in serum
- for total bile salts assay using an enzymatic method
3α-Hydroxysteroid dehydrogenase (3α-HSD) plays a crucial physiological role in vivo, responsible for inactivating circulating steroid hormones and regulating their activity in target tissues (especially the liver), thus participating in steroid hormone clearance. In vitro, purified 3α-HSD is widely used as a biochemical reagent, primarily for clinical diagnosis and research. For example, it can be used to determine enzyme activity levels for quantitative analysis of bile acid or certain steroid hormone levels. Furthermore, it is an important tool for studying the mechanisms of action of nonsteroidal anti-inflammatory drugs (NSAIDs) and progestins, as these drugs are often found to be inhibitors of this enzyme.
3α-hydroxysteroid dehydrogenase (3α-HSD) may help to modulate the occupancy of the androgen receptor (AR) in androgen target tissues. It may also act in hindering androgen action.
