Abstract
The α and β isomers of spiro-3-oxiranyl-5α-androstan-17β-ol were tested as possible inhibitors of Δ5-3-ketosteroid isomerase of Pseudomonas testosteroni. The β-oxirane causes a first-order irreversible inactivation of the enzyme and shows saturation kinetics (KI, 17 μM). Protection against inactivation is exhibited by 19-nortestosterone, a competitive inhibitor of the isomerase. Although the α-oxirane was found to be a good reversible inhibitor (Ki, 21 μM), prolonged incubation with it failed to produce any inactivation of the isomerase. The results obtained are consistent with the presence of a nucleophilic group situated near the 3-keto group of the substrate in the enzyme-steroid complex.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 783-790 |
| Number of pages | 8 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 91 |
| Issue number | 3 |
| DOIs | |
| State | Published - Dec 14 1979 |
| Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
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Pollack, R. M., Kayser, R. H., & Bevins, C. L. (1979). An active-site-directed irreversible inhibitor of Δ5-3-ketosteroid isomerase. Biochemical and Biophysical Research Communications, 91(3), 783-790. https://doi.org/10.1016/0006-291X(79)91948-X