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Published January 31, 2015 | Version v1
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Purification of Δ -3-ketosteroid isomerase from Digitalis lanata

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  • 1. Friedrich-Alexander-Universität, Lehrstuhl für Pharmazeutische Biologie, Staudtstr. 5, D-91058 Erlangen, Germany

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Meitinger, Nadine, Geiger, Daniel, Augusto, Thierry W., Pádua, Rodrigo Maia de, Kreis, Wolfgang (2015): Purification of Δ -3-ketosteroid isomerase from Digitalis lanata. Phytochemistry 109: 6-13, DOI: 10.1016/j.phytochem.2014.10.025, URL: http://dx.doi.org/10.1016/j.phytochem.2014.10.025

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urn:lsid:plazi.org:pub:B678FFEDFFDEFFFCD36E0633FFB5ED4A

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Figure: 10.5281/zenodo.10488220 (DOI)
Figure: 10.5281/zenodo.10488222 (DOI)
Figure: 10.5281/zenodo.10488224 (DOI)
Figure: 10.5281/zenodo.10488228 (DOI)
Figure: 10.5281/zenodo.10488230 (DOI)
Figure: 10.5281/zenodo.10488232 (DOI)

References

  • Batzold, F.H., Benson, A.M., Covey, D.F., Robinson, C.H., Talalay, P., 1976. The Δ5-3- ketosteroid isomerase reaction: catalytic mechanism, specificity and inhibition. Adv. Enzyme Regul. 14, 243-267.
  • Bradford, M.M., 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1), 248-254.
  • Campbell, M., Hahn, F.M., Poulter, C.D., Leustek, T., 1998. Analysis of the isopentenyl diphosphate isomerase gene family from Arabidopsis thaliana. Plant Mol. Biol. 36 (2), 323-328.
  • Chiang, Y.R., Ismail, W., Gallien, S., Heintz, D., Van Dorsselaer, A., Fuchs, G., 2008a. Cholest-4-en-3-one-Δ1-dehydrogenase, a flavoprotein catalyzing the second step in anoxic cholesterol metabolism. Appl. Environ. Microbiol. 74 (1), 107- 113.
  • Chiang, Y.R., Ismail, W., Heintz, D., Schaeffer, C., Van Dorsselaer, A., Fuchs, G., 2008b. Study of anoxic and oxic cholesterol metabolism by Sterolibacterium denitrificans. J. Bacteriol. 190 (3), 905-914.
  • Croteau, R.B., Davis, E.M., Ringer, K.L., Wildung, M.R., 2005. (-)-Menthol biosynthesis and molecular genetics. Naturwissenschaften 92 (12), 562-577.
  • Djerassi, C., Engle, R.R., Bowers, A., 1956. Notes-the direct conversion of steroidal Δ5-3β- alcohols to Δ5-and Δ4-3-ketones. J. Org. Chem. 21 (12), 1547-1549.
  • Finsterbusch, A., Lindemann, P., Grimm, R., Eckerskorn, C., Luckner, M., 1999. Δ5- 3β- Hydroxysteroid dehydrogenase from Digitalis lanata Ehrh.-a multifunctional enzyme in steroid metabolism? Planta 209 (4), 478-486.
  • Gollwitzer, J., Lenz, R., Hampp, N., Zenk, M.H., 1993. The transformation of neopinoneto codeinone in morphine biosynthesis proceeds non-enzymatically. Tetrahedron Lett. 34 (36), 5703-5706.
  • Ha, N.C., Choi, G., Choi, K.Y., Oh, B.H., 2001. Structure and enzymology of Δ5-3- ketosteroid isomerase. Curr. Opin. Struct. Biol. 11 (6), 674-678.
  • Herl, V., Frankenstein, J., Meitinger, N., Muller-Uri, F., Kreis, W., 2007. Δ5-3β- Hydroxysteroid dehydrogenase (3βHSD) from Digitalis lanata. Heterologous expression and characterisation of the recombinant enzyme. Planta Med. 73 (7), 704.
  • Heukeshoven, J., Dernick, R., 1985. Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining. Electrophoresis 6 (3), 103-112.
  • Houck, W.J., Pollack, R.M., 2003. Activation enthalpies and entropies for the microscopic rate constants of acetate-catalyzed isomerization of 5-androstene- 3, 17-dione. J. Am. Chem. Soc. 125 (34), 10206-10212.
  • Johansson, A.S., Mannervik, B., 2001. Human glutathione transferase A3-3, a highly efficient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones. J. Biol. Chem. 276 (35), 33061-33065.
  • Jones, J.B., Wigfield, D.C., 1969. Steroids and steroidases. IX. Activation parameters and the mechanism of base-and enzyme-catalyzed isomerizations of androst-5- ene-3, 17-dione. The nature of the active center of the Δ5+Δ4-3-ketosteroid isomerase of Pseudomonas testosteroni. Can. J. Chem. 47 (23), 4459-4466.
  • Jork, H., Funk, W., Fischer, W., Wimmer, H., 1990. Thin-Layer Chromatography: Reagents and Detection Methods, Vol. 1a. VCH.
  • Kjonaas, R.B., Venkatachalam, K.V., Croteau, R., 1985. Metabolism of monoterpenes: oxidation of isopiperitenol to isopiperitenone, and subsequent isomerization to piperitenone by soluble enzyme preparations from peppermint (Mentha piperita) leaves. Arch. Biochem. Biophys. 238 (1), 49-60.
  • Kreis, W., Muller-Uri, F., 2013. Cardenolide aglycone formation in Digitalis. In: Isoprenoid Synthesis in Plants and Microorganisms. Springer, New York, pp. 425-438.
  • Kreis, W., Reinhard, E., 1988. 12β- Hydroxylation of digitoxin by suspension-cultured Digitalis lanata cells. production of deacetyllanatoside c using a two- Stage culture method 1. Planta Med. 54 (02), 143-148.
  • Krozowski, Z., 1994. The short-chain alcohol dehydrogenase superfamily: variations on a common theme. J. Steroid Biochem. Mol. Biol. 51 (3), 125-130.
  • Lindemann, P., Finsterbusch, A., Pangert, A., Luckner, M., 2000. Partial cloning of a Δ5-3β- hydroxysteroid dehydrogenase from Digitalis lanata. In: Okamoto, M., Ishimura, Y., Nawata, H. (Eds.), Molecular Steroidogenesis, Proceedings of the Yamada Conference LII, Vol. 29. Frontiers Science Series, pp. 333-334.
  • Malhotra, S.K., Ringold, H.J., 1965. Chemistry of conjugate anions and enols. V. Stereochemistry, kinetics, and mechanism of the acid- and enzymatic-catalyzed isomerization of 5-3-keto steroids 1,2. J. Am. Chem. Soc. 87 (14), 3228-3236.
  • Munkert, J., Ernst, M., Muller-Uri, F., Kreis, W., 2014. Identification and stressinduced expression of three 3β- hydroxysteroid dehydrogenases from Erysimum crepidifolium Rchb. and their putative role in cardenolide biosynthesis. Phytochemistry 100, 26-33.
  • Newman, R.A., Yang, P., Pawlus, A.D., Block, K.I., 2008. Cardiac glycosides as novel cancer therapeutic agents. Mol. Interventions 8 (1), 36.
  • Pichersky, E., Gang, D.R., 2000. Genetics and biochemistry of secondary metabolites in plants: an evolutionary perspective. Trends Plant Sci. 5 (10), 439-445.
  • Pollack, R.M., 2004. Enzymatic mechanisms for catalysis of enolization: ketosteroid isomerase. Bioorg. Chem. 32 (5), 341-353.
  • Prassas, I., Diamandis, E.P., 2008. Novel therapeutic applications of cardiac glycosides. Nat. Rev. Drug Discovery 7 (11), 926-935.
  • Rasband, W.S., ImageJ, U. S. National Institutes of Health, Bethesda, Maryland, USA, http://imagej.nih.gov/ij/, 1997-2014.
  • Seidel, S., Kreis, W., Reinhard, E., 1990. 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. Plant Cell Rep. 8 (10), 621-624.
  • Smith, S.B., Richards, J.W., Benisek, W.F., 1980. The purification and characterization of Δ5-3-ketosteroid isomerase from Pseudomonas putida, a cysteine-containing isomerase. J. Biol. Chem. 255 (7), 2678-2684.
  • Talalay, P., Wang, V.S., 1955. Enzymic isomerization of Δ5-3-ketosteroids. Biochim. Biophys. Acta 18, 300-301.
  • Thomas, J.L., Frieden, C., Nash, W.E., Strickler, R.C., 1995. An NADH-induced conformational change that mediates the sequential 3-hydroxysteroid dehydrogenase/isomerase activities is supported by affinity labeling and the time-dependent activation of isomerase. J. Biol. Chem. 270 (36), 21003-21008.
  • Yang, X., Dubnau, E., Smith, I., Sampson, N.S., 2007. Rv1106c from Mycobacterium tuberculosis is a 3β- hydroxysteroid dehydrogenase. Biochemistry 46 (31), 9058- 9067.

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