Creative Enzymes provides the efficient, accurate and precise activity measurement of 3alpha-hydroxysteroid 3-dehydrogenase. With persistent effort in enzyme research and consistent service quality, Creative Enzymes has earned the best trust and compliment from countless customers. We are continuing our enzyme research and development with more and more breakthroughs to meet the requirements from the industry.

3Alpha-hydroxysteroid 3-dehydrogenase (Si-specific) (EC1.1.1.50; 3α-HSDH) is a class of enzyme that catalyzes the reversible oxidoreduction reaction between 3alpha-hydroxysteroid and 3-oxosteroid. It generates NAD(P)H simultaneously which acts as a hydrogen donor for many biosynthetic processes. This enzyme exists not only in bacteria, such as Pseudomonas sp. and Eubacterium sp., but also in eukarya, such as human, mouse and bovine. 3Alpha-hydroxysteroid 3-dehydrogenase (Si-specific) belongs to the family of oxidoreductases, In particular, it is the oxidoreductase that catalyzes the CH-OH group of the substrate and uses NAD⁺ or NADP⁺ as the cofactor. So more specifically 3alpha-hydroxysteroid 3-dehydrogenase is a member of hydroxysteroid dehydrogenases. The systematic name of this enzyme class is 3alpha-hydroxysteroid: NAD(P)⁺ oxidoreductase (B-specific), which is also known as:

• hydroxyprostaglandin dehydrogenase;
• 3alpha-hydroxysteroid oxidoreductase;
• sterognost 3alpha;
• 3alpha-hydroxysteroid dehydrogenase (B-specific);
• 3alpha-hydroxysteroid 3-dehydrogenase (B-specific)

As a broadly used enzyme, 3alpha-hydroxysteroid 3-dehydrogenase (Si-specific) functions via three metabolic pathways: primary bile acid biosynthesis, c21-steroid hormone metabolism, and androgen and estrogen metabolism. The transformation of androstendione from testosterone and androsterone degradation are the critical steps in androgen and estrogen metabolism. Both testosterone and androsterone are the sole carbon and energy source for certain microorganisms, such as Comamonas testosteroni. In Comamonas testosterone, degradation of testosterone is initiated by dehydrogenation of the 17β-hydroxyl group to androst-4-ene-3,17-dione, and degradation of androsterone is initiated by the same transformation, which has to be catalyzed by 3α-hydroxysteroid dehydrogenase or the other dehydrogenases. A number of substrates can be utilized by 3alpha-hydroxysteroid 3-dehydrogenase (Si-specific) including 1-acenaphthenol, 17beta-estradiol, 3-hydroxysteroid, 3-oxocholic acid, 5alpha-androstan-3,17-dione, etc.

Due to the diversity of substrates, the activity assay using spectrophotometry of 3alpha-hydroxysteroid 3-dehydrogenase (Si-specific) has not been difficult to set up in industry applications. With years of in-depth investigation, Creative Enzymes has enough confidence in providing the first-in-class service in the enzyme activity measurement. Creative Enzymes is the leading company in enzymological sciences and technologies and will satisfy the clients with customization services.

Figure: The three-dimensional structure of the 3alpha-hydroxysteroid dehydrogenase monomer from Comamonas testosteroni with bound NAD⁺ cosubstrate.
Reference: Clemens Grimm et al. J. Biol. Chem. 2000, 275:41333-41339