63-01-4

Basic information

• Product Name: 19-HYDROXYTESTOSTERONE-19-CME
• Synonyms: 4-ANDROSTEN-17-BETA, 19-DIOL-3-ONE-19-CARBOXYMETHYLETHER;19-HYDROXYTESTOSTERONE-19-CME;16-hydroxytestosterone;16A hydroxytestosterone--dea schedule*iii item;16A-HYDROXYTESTOSTERONE;4-Androstene-16ALPHA,17B-diol-3-one;16α, 17β-Dihydroxyandrost-4-en-3-one, 4-Androstene-16α,17β-diol-3-one;16α,17β-Dihydroxyandrost-4-en-3-one
• CAS NO: 63-01-4
• Molecular Formula: C19H28O3
• Molecular Weight: 304.43
• Mol File: 63-01-4.mol
• Article Data: 7

Chemical Properties

• Melting Point: 192-194 °C
• Boiling Point: 454.7°C at 760 mmHg
• Flash Point: 242.9°C
• Appearance: /
• Density: 1.19g/cm³
• Vapor Pressure: 3.53E-10mmHg at 25°C
• Refractive Index: 1.578
• Storage Temp.: 2-8°C
• CAS DataBase Reference: 19-HYDROXYTESTOSTERONE-19-CME(CAS DataBase Reference)
• NIST Chemistry Reference: 19-HYDROXYTESTOSTERONE-19-CME(63-01-4)
• EPA Substance Registry System: 19-HYDROXYTESTOSTERONE-19-CME(63-01-4)

Safety Data

• Hazard Codes: Xn
• Statements: 61-40-20/21/22-63
• Safety Statements: 53-22-36/37/39-36/37
• Hazardous Substances Data: 63-01-4(Hazardous Substances Data)

Usage

Uses

Different sources of media describe the Uses of 63-01-4 differently. You can refer to the following data:
1. 16α-Hydroxytestosterone is an metabolite of Testosterone (T155000), the major circulating androgen. Testosterone was found to be metabolized by cytochrome P-450 to 16α-Hydroxytestosterone in rat liver .
2. 19-Hydroxytestosterone-19-CME is a derivative of 19-Hydroxyandrostendione (H801500), a novel substituted estrogen as aromatase inhibitor. It induces neuroendocrine trans-differentiation of prostate cancer cells via an ectopic olactory receptor.

InChI:InChI=1/C19H28O3/c1-18-7-5-12(20)9-11(18)3-4-13-14(18)6-8-19(2)15(13)10-16(21)17(19)22/h9,13-17,21-22H,3-8,10H2,1-2H3

Upstream product

• 58-22-0 testosterone 
• 975-00-8 16α,17β-Dihydroxy-3-ethoxy-androstadien-(3,5) 
• 1096-38-4 16-dehydroprogesterone 
• 595-77-7 R-16α,17-dihydroxy-pregn-4-ene-3,20-dione 
• 1594-52-1 16α-acetoxy-17-hydroxy-pregn-4-ene-3,20-dione 
• 981-68-0 16α-Acetoxy-3-ethoxy-androstadien-(3,5)-on-(17) 
• 96580-28-8 17α-Hydroxy-3-ethoxy-16α-acetoxy-pregnadien-3,5-on-(20) 
• 987-16-6 17α-Hydroxy-3-ethoxy-16α-acetoxy-pregnadien-3,5-on-20-oxim 

Relevant articles and documents

Tracking Down a New Steroid-Hydroxylating Promiscuous Cytochrome P450: CYP154C8 from Streptomyces sp. W2233-SM

CYP154C8 from Streptomyces sp. has been identified as a new cytochrome P450 with substrate flexibility towards different sets of steroids. In vitro treatment of these steroids with CYP154C8 revealed interesting product formation patterns with the same group of steroids. NMR study revealed the major product of corticosterone to be hydroxylated at the C21 position, whereas progesterone, androstenedione, testosterone, and 11-ketoprogesterone were exclusively hydroxylated at the 16α position. However, the 16α-hydroxylated product of progesterone was further hydroxylated to yield dihydroxylated products. 16-hydroxyprogesterone was hydroxylated at two positions to yield dihydroxylated products: 2α,16α-dihydroxyprogesterone and 6β,16α-dihydroxyprogesterone. To the best of our knowledge, this is the first report of generation of such products through enzymatic hydroxylation by a CYP450. In view of the importance of modified steroids as pharmaceutical components, CYP154C8 has immense potential for utilization in bioproduction of hydroxylated derivative compounds to be directly employed for pharmaceutical applications.

Characterization of two steroid hydroxylases from different Streptomyces spp. and their ligand-bound and -unbound crystal structures

Bacterial cytochrome P450 (CYP) enzymes are involved in the hydroxylation of various endogenous substrates while using a heme molecule as a cofactor. CYPs have gained biotechnological interest as useful biocatalysts capable of altering chemical structures by adding a hydroxyl group in a regiospecific manner. Here, we identified, purified, and characterized two CYP154C4 proteins from Streptomyces sp. W2061 (StCYP154C4-1) and Streptomyces sp. ATCC 11861 (StCYP154C4-2). Activity assays showed that both StCYP154C4-1 and StCYP154C4-2 can produce 2′-hydroxylated testosterone, which differs from the activity of a previously described NfCYP154C5 from Nocardia farcinica in terms of its 16α-hydroxylation of testosterone. To better understand the molecular basis of the regioselectivity of these two CYP154C4 proteins, crystal structures of the ligand-unbound form of StCYP154C4-1 and the testosterone-bound form of StCYP154C4-2 were determined. Comparison with the previously determined NfCYP154C5 structure revealed differences in the substrate-binding residues, suggesting a likely explanation for the different patterns of testosterone hydroxylation, despite the high sequence similarities between the enzymes (54% identity). These findings provide valuable insights that will enable protein engineering for the development of artificial steroid-related CYPs exhibiting different regiospecificity.

A Peroxygenase from Chaetomium globosum Catalyzes the Selective Oxygenation of Testosterone

Unspecific peroxygenases (UPO, EC 1.11.2.1) secreted by fungi open an efficient way to selectively oxyfunctionalize diverse organic substrates, including less-activated hydrocarbons, by transferring peroxide-borne oxygen. We investigated a cell-free approach to incorporate epoxy and hydroxyl functionalities directly into the bulky molecule testosterone by a novel unspecific peroxygenase (UPO) that is produced by the ascomycetous fungus Chaetomium globosum in a complex medium rich in carbon and nitrogen. Purification by fast protein liquid chromatography revealed two enzyme fractions with the same molecular mass (36 kDa) and with specific activity of 4.4 to 12 U mg?1. Although the well-known UPOs of Agrocybe aegerita (AaeUPO) and Marasmius rotula (MroUPO) failed to convert testosterone in a comparative study, the UPO of C. globosum (CglUPO) accepted testosterone as substrate and converted it with total turnover number (TTN) of up to 7000 into two oxygenated products: the 4,5-epoxide of testosterone in β-configuration and 16α-hydroxytestosterone. The reaction performed on a 100 mg scale resulted in the formation of about 90 % of the epoxide and 10 % of the hydroxylation product, both of which could be isolated with purities above 96 %. Thus, CglUPO is a promising biocatalyst for the oxyfunctionalization of bulky steroids and it will be a useful tool for the synthesis of pharmaceutically relevant steroidal molecules.