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Plurypotency of 17[beta]-hydroxysteroid dehydrogenase from the filamentous fungus Cochliobolus lunatusZorko, Matjaž, 1947- ; Gottlieb, H... E. ; Žakelj-Mavrič, MarijaCochliobolus lunatus 17B-hydroxysteroid dehydrogenase (17B-HSD) is pluripotentfor 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-substratecomplex into the corresponding products. As suggestedby the competition studies quinones and 17-ketosteroids are convertedby 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 17B-HSD is the first known fungal pluripotent enzyme of this type.Vir: Steroids. - ISSN 0039-128X (Letn. 65, 2000, str. 46-53)Vrsta gradiva - članek, sestavni delLeto - 2000Jezik - angleškiCOBISS.SI-ID - 11161817
Avtor
Zorko, Matjaž, 1947- |
Gottlieb, H... E. |
Žakelj-Mavrič, Marija
Teme
Ascomycetes |
Chemistry |
Enzymology |
17-hydroxysteroid dehydrogenases |
Binding sites |
Binding, competitive |
Nadph dehydrogenase |
Kinetics |
Spectrum analysis, mass |
Nuclear magnetic resonance |
Substrate specificity |
Steroids |
Androstenedione |
Vitamin k |
Quinones
Vnos na polico
Trajna povezava
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| Leto | Faktor vpliva | Izdaja | Kategorija | Razvrstitev | ||||
|---|---|---|---|---|---|---|---|---|
| JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP | |
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Baze podatkov, v katerih je revija indeksirana
| Ime baze podatkov | Področje | Leto |
|---|
| Povezave do osebnih bibliografij avtorjev | Povezave do podatkov o raziskovalcih v sistemu SICRIS |
|---|---|
| Zorko, Matjaž, 1947- | 04350 |
| Žakelj-Mavrič, Marija | 03082 |
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