15981-54-1

Basic information

• Product Name: 9α-Hydroxyprogesterone
• Synonyms: 9-Hydroxypregn-4-ene-3,20-dione;9-Hydroxyprogesterone;9α-Hydroxyprogesterone
• CAS NO: 15981-54-1
• Molecular Formula: C₂₁H₃₀O₃
• Molecular Weight: 330.46
• Mol File: 15981-54-1.mol
• Article Data: 5

Chemical Properties

• Melting Point: 190-192 °C
• Boiling Point: 482.9±45.0 °C(Predicted)
• Appearance: /
• Density: 1.15±0.1 g/cm3(Predicted)
• PKA: 14.20±0.70(Predicted)
• CAS DataBase Reference: 9α-Hydroxyprogesterone(CAS DataBase Reference)
• NIST Chemistry Reference: 9α-Hydroxyprogesterone(15981-54-1)
• EPA Substance Registry System: 9α-Hydroxyprogesterone(15981-54-1)

Safety Data

• Hazardous Substances Data: 15981-54-1(Hazardous Substances Data)

Upstream product

• 57-83-0 Progesterone 

Downstream Products

• 17652-16-3 pregna-4,9⁽¹¹⁾-diene-3,20-dione 
• 83603-61-6 pregna-4,8⁽⁹⁾-diene-3,20-dione 
• 560-62-3 9-alpha-hydroxyandrost-4-ene-3,17-dione 

Relevant articles and documents

Engineering of CYP106A2 for steroid 9α- and 6β-hydroxylation

CYP 106A2 from Bacillus megaterium ATCC 13368 has been described as a 15β-hydroxylase showing also minor 11α-, 9α- and 6β-hydroxylase activity for progesterone conversion. Previously, mutant proteins with a changed selectivity towards 11α-OH-progesterone have already been produced. The challenge of this work was to create mutant proteins with a higher regioselectivity towards hydroxylation at positions 9 and 6 of the steroid molecule. 9α-hydroxyprogesterone exhibits pharmaceutical importance, because it is a useful intermediate in the production of physiologically active substances which possess progestational activity. Sixteen mutant proteins were selected from a library containing mutated proteins created by a combination of site-directed and saturation mutagenesis of active site residues. Four mutant proteins out of these catalyzed the conversion of progesterone to 9α-OH-progesterone as a main product. For further optimization site-directed mutagenesis was performed. The introduction of seven mutations (D217V, A243V, A106T, F165L, T89N, T247V or T247W) into these four mutant proteins led to 28 new variants, which were also used for an in vivo conversion of progesterone. The best mutant protein, F165L/A395E/G397V, showed a ten-fold increase in the selectivity towards progesterone 9α-hydroxylation compared with the wild type CYP106A2. Also 6β-OH-progesterone is a pharmaceutically important compound, especially as intermediate for the production of drugs against breast cancer. For the rational design of mutant proteins with 6β-selectivity, docking of the 3D-structure of CYP106A2 with progesterone was performed. The introduction of three mutations (T247A, A243S, F173A) led to seven new mutant proteins. Clone A243S showed the greatest improvement in 6β-selectivity being more than ten-fold. Finally, an in vivo conversion of 11-deoxycorticosterone (DOC), testosterone and cortisol with the best five mutant proteins displaying 9α- or 6β-hydroxylation, respectively, of progesterone was performed to investigate whether the introduced mutations also effected the conversion of other substrates.

Biotransformations of progesterone by Chlorella spp.

Thirty-eight strains of Chlorella spp. were used as bioreactors on progesterone. Fourteen strains were ineffective whilst the others biotransformed the substrate. The observed bioreactions for progesterone were the hydroxylation, the reduction and the side-chain degradation. The kinds of biotransformation seem to fit the actual classification of the strains.

Progesterone bioconversion by microalgal cultures

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