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digitalis lanata/progesterone
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Progesterone: its possible role in the biosynthesis of cardenolides in Digitalis lanata.
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The incorporation of progestrone-7alpha-(3)H and pregnenolone-7alpha-(3)H into digitoxigenin, gitoxigenin, and digoxigenin in isolated, surviving leaves of Digitalis lanata was demonstrated. In addition, the conversion of pregnenolone to progesterone in the same system was proved. The results tend
Truncation of N-terminal regions of Digitalis lanata progesterone 5β-reductase alters catalytic efficiency and substrate preference.
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N-Terminal truncated forms of progesterone 5β-reductase (P5βR) were synthesized taking a full-length cDNA encoding for Digitalis lanata P5βR with a hexa-histidine tag attached at the C-terminus (rDlP5βRc) as the starting point. Four pETite-c-His/DlP5βR constructs coding for P5βR derivatives
Characterization and localization of progesterone 5 alpha-reductase from cell cultures of foxglove (Digitalis lanata EHRH).
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Progesterone 5 alpha-reductase, which catalyses the reduction of progesterone to 5 alpha-pregnane-3,20-dione, was isolated and characterized from cell cultures of Digitalis lanata (foxglove). Optimum enzyme activity was observed at pH 7.0, and the enzyme had an apparent Km value of 30 microM for its
Expression of 3beta-HSD and P5betaR, genes respectively coding for Delta5-3beta-hydroxysteroid dehydrogenase and progesterone 5beta-reductase, in leaves and cell cultures of Digitalis lanata EHRH.
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Plants of the genus Digitalis produce 5 beta-cardenolides that are used in the therapy of cardiac insufficiency in humans. 3 beta-Hydroxysteroid dehydrogenase (3 beta-HSD) and progesterone 5 beta-reductase (P5 betaR) are both supposed to be important enzymes in the biosynthesis of these natural
The crystal structure of progesterone 5beta-reductase from Digitalis lanata defines a novel class of short chain dehydrogenases/reductases.
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Progesterone 5beta-reductase (5beta-POR) catalyzes the stereospecific reduction of progesterone to 5beta-pregnane-3,20-dione and is a key enzyme in the biosynthetic pathway of cardenolides in Digitalis (foxglove) plants. Sequence considerations suggested that 5beta-POR is a member of the short chain
Molecular cloning and heterologous expression of progesterone 5beta-reductase from Digitalis lanata Ehrh.
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A full-length cDNA clone that encodes progesterone 5beta-reductase (5beta-POR) was isolated from Digitalis lanata leaves. The reading frame of the 5beta-POR gene is 1170 nucleotides corresponding to 389 amino acids. For expression, a Sph1/Sal1 5beta-POR fragment was cloned into the pQE vector and
Crystallization and preliminary crystallographic analysis of selenomethionine-labelled progesterone 5beta-reductase from Digitalis lanata Ehrh.
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Progesterone 5beta-reductase (5beta-POR) catalyzes the reduction of progesterone to 5beta-pregnane-3,20-dione and is the first stereospecific enzyme in the putative biosynthetic pathway of Digitalis cardenolides. Selenomethionine-derivatized 5beta-POR from D. lanata was successfully overproduced and
Conversion of sitosterol to progesterone by Digitalis lanata.
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The role of deoxycorticosterone in the biosynthesis of cardenolides in Digitalis lanata.
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The role of deoxycorticosterone in the biosynthesis of digitoxigenin was investigated by the simultaneous administration of deoxy[1,2-(3)H(2)]corticosterone and [4-(14)C]progesterone to a Digitalis lanata plant. The biosynthetically formed [(3)H,(14)C]digitoxigenin and
Δ5-3β-hydroxysteroid dehydrogenase/Δ5-Δ4-ketosteroid isomerase (3β-HSD), a possible enzyme of cardiac glycoside biosynthesis, in cell cultures and plants of Digitalis lanata EHRH.
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The in vitro transformation of pregnenolone into progesterone in Digitalis lanata tissues was shown to be catalyzed by a 3β-hydroxysteroid dehydrogenase/ketosteroid isomerase (3β-HSD). Product formation was monitored by HPLC. The enzyme could be partially characterized and 3β-HSD activities were
3 alpha-Hydroxysteroid-5 beta-oxidoreductase in tissue cultures of Digitalis lanata.
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Putative intermediates of cardenolide biosynthesis, namely progesterone, pregnenolone, 5 beta-pregnane-3,20-dione or 5 beta-pregnan-3 beta-ol-20-one, were administered to light- or dark-grown shoot cultures of Digitalis lanata. The unsaturated compounds were reduced to their respective 5
Progesterone 5β-reductase genes of the Brassicaceae family as function-associated molecular markers.
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This study aimed to define progesterone 5β-reductases (P5βR, EC 1.3.99.6, enone 1,4-reductases) as function-associated molecular markers at the plant family level. Therefore cDNAs were isolated from 25 Brassicaceae species, including two species, Erysimum crepidifolium and Draba aizoides, known to
Molecular cloning and expression of progesterone 5beta-reductase (5beta-POR) from Isoplexis canariensis.
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A full-length cDNA clone that encodes progesterone 5beta-reductase (5beta-POR, EC 1.3.1.3) was isolated from ISOPLEXIS CANARIENSIS leaves. The reading frame of the IC5beta-POR gene is 1170 nucleotides corresponding to 389 amino acids. The SPHI /SALI IC5beta-POR fragment was cloned into the pQE
Progesterone 5β-reductases/iridoid synthases (PRISE): gatekeeper role of highly conserved phenylalanines in substrate preference and trapping is supported by molecular dynamics simulations.
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Vein Patterning 1 (VEP1)-encoded progesterone 5β-reductases/iridoid synthases (PRISE) belong to the short-chain dehydrogenase/reductase superfamily of proteins. They are characterized by a set of highly conserved amino acids in the substrate-binding pocket. All PRISEs are capable of reducing the
Progesterone 5β-reductase of Erysimum crepidifolium: cDNA cloning, expression in Escherichia coli, and reduction of enones with the recombinant protein.
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Erysimum is a genus of the Brassicaceae family closely related to the genus Arabidopsis. Several Erysimum species accumulate 5β-cardenolides. Progesterone 5β-reductases (P5βRs) first described in Digitalis species are thought to be involved in 5β-cardenolide biosynthesis. P5βRs belong to the
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