Norcholanic acids as substrates for recombinant 3β-hydroxysteroid dehydrogenase and progesterone 5β-reductase, enzymes of the 5β-cardenolide biosynthesis |
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| Authors: | Pia Schebitz Andreas Hensel Wolfgang Kreis |
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| Institution: | a Lehrstuhl für Pharmazeutische Biologie, Department für Biologie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Staudtstrasse 5, 91058 Erlangen, Germany
b Institut für Pharmazeutische Biologie und Phytochemie Westfälische Wilhelms-Universität Münster, Hittorfstrasse 56, 48149 Münster, Germany |
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| Abstract: | The conversion of 23-nor-5,20(22)E-choladienic acid-3β-ol and other intermediates of the putative norcholanic acid pathway of cardenolide biosynthesis by recombinant 3β-hydroxysteroid dehydrogenase from Digitalis lanata in dehydrogenation and reduction reactions was investigated. 23-nor-4,20(22)E-choladienic acid-3-one was found to be a substrate of recombinant progesterone 5β-reductases from D. lanata and Arabidopsis thaliana. The role of various substrates in cardenolide biosynthesis is discussed. |
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| Keywords: | Cardenolide biosynthesis Enzyme catalysis 3β-Hydroxysteroid dehydrogenase Norcholanic acid Progesterone 5β-reductase Short-chain dehydrogenase/reductase |
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