Abstract
Cochliobolus lunatus 17β-hydroxysteroid dehydrogenase (17β-HSD) is pluripotent for several steroidal and nonsteroidal substrates. In the presence of NADPH the enzyme was found to reduce 3-keto groups of 4,5-dihydro steroids, 20-keto groups, and most efficiently, 17-keto groups of steroidal substrates. In addition, several quinones were accepted and found to be even better substrates as steroids due to their higher affinity for the enzyme-coenzyme complex and faster conversion of the enzyme-coenzyme-substrate complex into the corresponding products. As suggested by the competition studies quinones and 17-ketosteroids are converted by the same active center of the enzyme. For all tested substrates, the equilibrium ordered mechanism was established with NADPH binding first to the enzyme. According to our knowledge, the investigated 17β-HSD is the first known fungal pluripotent enzyme of this type. Copyright (C) 2000 Elsevier Science Inc.
| Original language | English |
|---|---|
| Pages (from-to) | 46-53 |
| Number of pages | 8 |
| Journal | Steroids |
| Volume | 65 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 2000 |
Bibliographical note
Funding Information:The authors wish to thank Dr D. Žigon from the Institute Joz̆ef Stefan for taking the mass spectra and M. Marušic̆ and K. Makovec for their skillful technical assistance. This work was supported by the Ministry of Science and Technology of Slovenia.
Funding
The authors wish to thank Dr D. Žigon from the Institute Joz̆ef Stefan for taking the mass spectra and M. Marušic̆ and K. Makovec for their skillful technical assistance. This work was supported by the Ministry of Science and Technology of Slovenia.
| Funders |
|---|
| Ministry of Science and Technology of Slovenia |
Keywords
- 17β-Hydroxysteroid dehydrogenase
- Carbonyl reductase
- Cochliobolus lunatus
- Fungi
- Kinetic analysis