The inducible and cytochrome P450-containing dehydroepiandrosterone 7α-hydroxylating enzyme system of Fusarium moniliforme 

@article{Cotillon1997TheIA,
  title={The inducible and cytochrome P450-containing dehydroepiandrosterone 7$\alpha$-hydroxylating enzyme system of Fusarium moniliforme
},
  author={A. C. Cotillon and Jaleh Doostzadeh and Robert Morfin},
  journal={The Journal of Steroid Biochemistry and Molecular Biology},
  year={1997},
  volume={62},
  pages={467-475}
}
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Hydroxylation of DHEA and its analogues by Absidia coerulea AM93. Can an inducible microbial hydroxylase catalyze 7α- and 7β-hydroxylation of 5-ene and 5α-dihydro C19-steroids?

Transformation of 3-hydroxy-steroids by Fusarium moniliforme 7α-hydroxylase

  • A. CotillonR. Morfin
  • Chemistry, Biology
    The Journal of Steroid Biochemistry and Molecular Biology
  • 1999

Hydroxylation of DHEA, androstenediol and epiandrosterone by Mortierella isabellina AM212. Evidence indicating that both constitutive and inducible hydroxylases catalyze 7α- as well as 7β-hydroxylations of 5-ene substrates.

Ketoconazole and cycloheximide inhibition studies suggest the presence of constitutive and substrate-induced hydroxylases in M. isabellina on the basis of time course analysis of theHydroxylation of DHEA and androstenediol.

The human cytochrome P4507B1: catalytic activity studies

Novel metabolites of dehydroepiandrosterone and progesterone obtained in Didymosphearia igniaria KCH 6670 culture

Screening of mycelial fungi for 7α- and 7β-hydroxylase activity towards dehydroepiandrosterone

In total, 481 fungal strains were screened for the ability to carry out 7(α/β)-hydroxylation of dehydroepiandrosterone (DHEA, 3β-hydroxy-5-androsten-17-one), and the majority of strains were able to introduce a hydroxyl group to position 7α.

Dehydroepiandrosterone Metabolites and their Interactions in Humans

The cytochrome P4507B1 responsible for 7alpha-hydroxy-DHEA production and 11beta-HSD1 are key enzymes for the modulation of glucocorticoid action in humans.

Transformations of 4- and 17α-substituted testosterone analogues by Fusarium culmorum

Dihydroxylation of dehydroepiandrosterone in positions 7α and 15α by mycelial fungi

Application of the revealed active strains of microorganisms opens prospects for the efficient production of key intermediates of synthesis of modern medical preparations.

Synthesis of 3β-hydroxy-androsta-5,7-dien-17-one from 3β-hydroxyandrost-5-en-17-one via microbial 7α-hydroxylation

References

SHOWING 1-10 OF 34 REFERENCES

Studies of the enzyme complex responsible for pregnenolone and dehydroepiandrosterone 7α-hydroxylation in mouse tissues

Neurosteroid metabolism. 7 alpha-Hydroxylation of dehydroepiandrosterone and pregnenolone by rat brain microsomes.

The quantitatively important metabolism to 7 alpha-OH compounds may contribute to the control of neurosteroid activity in brain, and derivatives of DHEA and PREG are known to be neuroactive.

Pregnenolone-7 beta-hydroxylating activities of yeast-expressed mouse cytochrome P450-1A1 and mouse-tissue microsomes.

Findings indicate that, in addition to unidentified P450, P450 1A1 is involved in 7 beta-hydroxylation of pregnenolone and may contribute in part to the production of the 7-Hydroxylated steroids necessary for activation of immune defenses.

Pregnenolone-7β-hydroxylating activity of human cytochrome P450-1A1

Characterisation of microsomal dehydroepiandrosterone 7-hydroxylase from rat liver.

Induction of peroxisomal β-oxidation enzymes by dehydroepiandrosterone and its sulfate in primary cultures of rat hepatocytes

Purification and properties of cytochrome P-450 (P-450lun) catalyzing steroid 11 beta-hydroxylation in Curvularia lunata.

Bioconversion of steroids by Cochliobolus lunatus—II. 11β-hydroxylation of 17α,21-dihydroxypregna-1,4-diene-3,20-dione 17-acetate in dependence of the inducer structure

Pregnenolone and dehydroepiandrosterone as precursors of native 7-hydroxylated metabolites which increase the immune response in mice

  • R. MorfinG. Courchay
  • Biology, Chemistry
    The Journal of Steroid Biochemistry and Molecular Biology
  • 1994

Steroid 1-dehydrogenation and side-chain degradation enzymes in the life cycle of Fusarium solani.