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Volumn 73, Issue 7, 2007, Pages 704-710

Δ5-3β-hydroxysteroid dehydrogenase (3βHSD) from Digitalis lanata. Heterologous expression and characterisation of the recombinant enzyme

Author keywords

5 3 hydroxysteroid dehydrogenase; 5 3 ketosteroid isomerase; Cardenolide biosynthesis; Digitalis lanata; Gene expression; Plantaginaceae; Pregnenolone; Progesterone

Indexed keywords

3 BETA HYDROXYSTEROID DEHYDROGENASE; 5 PREGNENE 3,20 DIONE; CARDENOLIDE; CARDIAC GLYCOSIDE; HYBRID PROTEIN; ISOPROGESTERONE; PREGNENOLONE; PROGESTERONE; RECOMBINANT ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; STEROID REDUCTASE; TESTOSTERONE; UNCLASSIFIED DRUG; 3(OR 17)BETA HYDROXYSTEROID DEHYDROGENASE; DELTA(5) 3 BETA HYDROXYSTEROID DEHYDROGENASE; DELTA(5)-3 BETA-HYDROXYSTEROID DEHYDROGENASE; DIGITALIS; PLANT DNA;

EID: 34447540345     PISSN: 00320943     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-2007-981537     Document Type: Article
Times cited : (43)

References (29)
  • 1
    • 34447502595 scopus 로고    scopus 로고
    • Luckner M, Wichtl M. In: Luckner M, Wichtl M, editors. Digitalis. Stuttgart: WVGmbH; 2000: 1-352.
    • Luckner M, Wichtl M. In: Luckner M, Wichtl M, editors. Digitalis. Stuttgart: WVGmbH; 2000: 1-352.
  • 2
    • 0031830211 scopus 로고    scopus 로고
    • Cardenolide biosynthesis in foxglove
    • Kreis W, Hensel A, Stuhlemmer U. Cardenolide biosynthesis in foxglove. Planta Med 1998; 64: 491-9.
    • (1998) Planta Med , vol.64 , pp. 491-499
    • Kreis, W.1    Hensel, A.2    Stuhlemmer, U.3
  • 3
    • 0039819972 scopus 로고
    • 4-ketosteroid isomerase (3β-HSD), a possible enzyme of cardiac glycoside biosynthesis, in cell cultures and plants of Digitalis lanata EHRH
    • 4-ketosteroid isomerase (3β-HSD), a possible enzyme of cardiac glycoside biosynthesis, in cell cultures and plants of Digitalis lanata EHRH. Plant Cell Rep 1990; 8: 621-4.
    • (1990) Plant Cell Rep , vol.8 , pp. 621-624
    • Seidel, S.1    Kreis, W.2    Reinhard, E.3
  • 4
    • 0032589562 scopus 로고    scopus 로고
    • 5-3β-Hydroxysteroid dehydrogenase from Digitalis lanata Ehrh - a multifunctional enzyme in steroid metabolism?
    • 5-3β-Hydroxysteroid dehydrogenase from Digitalis lanata Ehrh - a multifunctional enzyme in steroid metabolism? Planta 1999; 209: 479-86.
    • (1999) Planta , vol.209 , pp. 479-486
    • Finsterbusch, A.1    Lindemann, P.2    Grimm, R.3    Eckerskorn, C.4    Luckner, M.5
  • 5
    • 34447520706 scopus 로고    scopus 로고
    • 5-3β-hydroxysteroid dehydrogenase from Digitalis lanata. In: Okamoto M, Ishimura Y, Nawata, H, editors. Molecular steroidogenesis, Proceedings of the Yamada Conference LII Tokyo: Universal Academy Press, Frontiers Science Series 29 - XXIV; 2000: 333-4.
    • 5-3β-hydroxysteroid dehydrogenase from Digitalis lanata. In: Okamoto M, Ishimura Y, Nawata, H, editors. Molecular steroidogenesis, Proceedings of the Yamada Conference LII Tokyo: Universal Academy Press, Frontiers Science Series 29 - XXIV; 2000: 333-4.
  • 7
    • 0025883535 scopus 로고
    • Characteristics of short-chain alcohol dehydrogenases and related enzymes
    • Persson B, Krook M, Jörnvall H. Characteristics of short-chain alcohol dehydrogenases and related enzymes. Eur J Biochem 1991; 200: 537-43.
    • (1991) Eur J Biochem , vol.200 , pp. 537-543
    • Persson, B.1    Krook, M.2    Jörnvall, H.3
  • 9
    • 7844242678 scopus 로고
    • 12β-hydroxylation of digitoxin by Digitalis lanata cells. Production of deacetyllanatoside C in a 20-L air-lift bioreactor
    • Kreis W, Zhu W, Reinhard E. 12β-hydroxylation of digitoxin by Digitalis lanata cells. Production of deacetyllanatoside C in a 20-L air-lift bioreactor. Biotechnol Lett 1989; 11: 25-30.
    • (1989) Biotechnol Lett , vol.11 , pp. 25-30
    • Kreis, W.1    Zhu, W.2    Reinhard, E.3
  • 10
    • 0023903132 scopus 로고
    • 12β-hydroxylation of digitoxin by suspension-cultured Digitalis lanata cells. Production of deacetyllanatoside C using a two-stage culture method
    • Kreis W, Reinhard E. 12β-hydroxylation of digitoxin by suspension-cultured Digitalis lanata cells. Production of deacetyllanatoside C using a two-stage culture method. Planta Med 1988; 54: 95-100.
    • (1988) Planta Med , vol.54 , pp. 95-100
    • Kreis, W.1    Reinhard, E.2
  • 12
    • 0026165519 scopus 로고
    • A maize gene expressed during embryogenesis is ABA-inducible and highly conserved
    • Williams B, Tsang A. A maize gene expressed during embryogenesis is ABA-inducible and highly conserved. Plant Mol Biol 1991; 16: 919-23.
    • (1991) Plant Mol Biol , vol.16 , pp. 919-923
    • Williams, B.1    Tsang, A.2
  • 13
    • 0033911054 scopus 로고    scopus 로고
    • Overexpression and catalytic function of cyclophilin 18 from Digitalis lanata Ehrh
    • Müller-Uri F, Reva VA. Overexpression and catalytic function of cyclophilin 18 from Digitalis lanata Ehrh. Pharm Pharmacol Lett 2000; 10: 5-7.
    • (2000) Pharm Pharmacol Lett , vol.10 , pp. 5-7
    • Müller-Uri, F.1    Reva, V.A.2
  • 14
    • 30344460658 scopus 로고    scopus 로고
    • Molecular cloning and heterologous expression of progesterone 5β-reductase from Digitalis lanata Ehrh
    • Herl V, Fischer G, Müller-Uri F, Kreis W. Molecular cloning and heterologous expression of progesterone 5β-reductase from Digitalis lanata Ehrh. Phytochemistry 2006; 67: 25-31.
    • (2006) Phytochemistry , vol.67 , pp. 25-31
    • Herl, V.1    Fischer, G.2    Müller-Uri, F.3    Kreis, W.4
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72: 248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 16
    • 34447514535 scopus 로고    scopus 로고
    • Jork H. Thin Layer Chromatography: Reagents and Detection Methods, 1. In: Jork H., Funk W, Fischer W, editors. Thin-Layer-Chromatography. New York: VCH Publishers; 2004: 195-8.
    • Jork H. Thin Layer Chromatography: Reagents and Detection Methods, Vol. 1. In: Jork H., Funk W, Fischer W, editors. Thin-Layer-Chromatography. New York: VCH Publishers; 2004: 195-8.
  • 17
    • 20444474228 scopus 로고    scopus 로고
    • Monoterpene metabolism. Cloning, expression, and characterization of (-)-isopiperitenoI/(-)-carveol dehydrogenase of peppermint and spearmint
    • Ringer KL, Davis EM, Croteau R. Monoterpene metabolism. Cloning, expression, and characterization of (-)-isopiperitenoI/(-)-carveol dehydrogenase of peppermint and spearmint. Plant Physiol 2005; 137: 863-72.
    • (2005) Plant Physiol , vol.137 , pp. 863-872
    • Ringer, K.L.1    Davis, E.M.2    Croteau, R.3
  • 18
    • 0035918142 scopus 로고    scopus 로고
    • Secoisolariciresinol dehydrogenase purification, cloning, and functional expression
    • Xia Z-Q, Costa MA, Pélissier HC, Davin LB, Lewis NG. Secoisolariciresinol dehydrogenase purification, cloning, and functional expression. J Biol Chem 2001; 276: 12614-23.
    • (2001) J Biol Chem , vol.276 , pp. 12614-12623
    • Xia, Z.-Q.1    Costa, M.A.2    Pélissier, H.C.3    Davin, L.B.4    Lewis, N.G.5
  • 21
    • 34447558742 scopus 로고    scopus 로고
    • Characterization of a 3α-hydroxysteroid dehydrogenase/carbonyl reductase from the gram-negative bacterium Commamonas testosteroni
    • Oppermann UCT, Maser E. Characterization of a 3α-hydroxysteroid dehydrogenase/carbonyl reductase from the gram-negative bacterium Commamonas testosteroni. Eur J Biochem 1996; 209: 459-66.
    • (1996) Eur J Biochem , vol.209 , pp. 459-466
    • Oppermann, U.C.T.1    Maser, E.2
  • 22
    • 0031021249 scopus 로고    scopus 로고
    • Active site directed mutagenesis of 3β/17β-hydroxysteroid dehydrogenase establishes differential effects on short-chain dehydrogenase/reductase reactions
    • Oppermann UCT, Filling C, Berndt KD, Persson B, Benach J, Ladenstein R et al. Active site directed mutagenesis of 3β/17β-hydroxysteroid dehydrogenase establishes differential effects on short-chain dehydrogenase/reductase reactions. Biochemistry 1997; 36: 34-40.
    • (1997) Biochemistry , vol.36 , pp. 34-40
    • Oppermann, U.C.T.1    Filling, C.2    Berndt, K.D.3    Persson, B.4    Benach, J.5    Ladenstein, R.6
  • 23
    • 0024242392 scopus 로고
    • Human placental 3β-hydroxy-5-ene-steroid dehydrogenase and steroid 5-4-ene-isomerase: Purification from microsomes, substrate kinetics, and inhibition by product steroids
    • Thomas JL, Berko EA, Faustino A, Myers RP, Strickler RC. Human placental 3β-hydroxy-5-ene-steroid dehydrogenase and steroid 5-4-ene-isomerase: purification from microsomes, substrate kinetics, and inhibition by product steroids. J Steroid Biochem 1988; 31: 785-93.
    • (1988) J Steroid Biochem , vol.31 , pp. 785-793
    • Thomas, J.L.1    Berko, E.A.2    Faustino, A.3    Myers, R.P.4    Strickler, R.C.5
  • 24
    • 0037126640 scopus 로고    scopus 로고
    • Structure of bacterial 3β/17β-hydroxysteroid dehydrogenase at 1.2 A resolution: A model for multiple steroid recognition
    • Benach J, Filling C, Oppermann UC, Roversi P, Bricogne G, Berndt KD et al. Structure of bacterial 3β/17β-hydroxysteroid dehydrogenase at 1.2 A resolution: a model for multiple steroid recognition. Biochemistry 2002; 41: 4659-68.
    • (2002) Biochemistry , vol.41 , pp. 4659-4668
    • Benach, J.1    Filling, C.2    Oppermann, U.C.3    Roversi, P.4    Bricogne, G.5    Berndt, K.D.6
  • 25
    • 0039819973 scopus 로고    scopus 로고
    • Cardenolide formation and activity of pregnane-modifying enzymes in cell suspension cultures, shoot cultures and leaves of Digitalis lanata
    • Stuhlemmer U, Kreis W. Cardenolide formation and activity of pregnane-modifying enzymes in cell suspension cultures, shoot cultures and leaves of Digitalis lanata. Plant Physiol Biochem 1996; 34: 85-91
    • (1996) Plant Physiol Biochem , vol.34 , pp. 85-91
    • Stuhlemmer, U.1    Kreis, W.2
  • 26
    • 0009788203 scopus 로고
    • Enzymes is cardenolide-accumulating shoot cultures of Digitalis purpurea L
    • Seitz HU, Gartner DE. Enzymes is cardenolide-accumulating shoot cultures of Digitalis purpurea L. Plant Cell Tissue Organ Cult 1994; 38: 337-44.
    • (1994) Plant Cell Tissue Organ Cult , vol.38 , pp. 337-344
    • Seitz, H.U.1    Gartner, D.E.2
  • 27
    • 4644373998 scopus 로고    scopus 로고
    • Enzymatic mechanisms for catalysis of enolization: Ketosteroid isomerase
    • Pollack RM. Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase. Bioorg Chem 2004; 32: 341-53.
    • (2004) Bioorg Chem , vol.32 , pp. 341-353
    • Pollack, R.M.1
  • 28
    • 0041429615 scopus 로고    scopus 로고
    • Activation enthalpies and entropies for the microscopic rate constants of acetate-catalyzed isomerization of 5-androstene-3,17-dione
    • Houck WJ, Pollack RM. Activation enthalpies and entropies for the microscopic rate constants of acetate-catalyzed isomerization of 5-androstene-3,17-dione. J Am Chem Soc 2003; 125: 10206-12.
    • (2003) J Am Chem Soc , vol.125 , pp. 10206-10212
    • Houck, W.J.1    Pollack, R.M.2
  • 29
    • 0027959548 scopus 로고
    • The short-chain alcohol dehydrogenase superfamily: Variations on a common theme
    • Krozowski Z. The short-chain alcohol dehydrogenase superfamily: variations on a common theme. J. Steroid Biochem Mol Biol 1994; 51: 125-30.
    • (1994) J. Steroid Biochem Mol Biol , vol.51 , pp. 125-130
    • Krozowski, Z.1


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