메뉴 건너뛰기




Volumn 54, Issue 3, 2008, Pages 388-401

The functional divergence of short-chain dehydrogenases involved in tropinone reduction

Author keywords

Brassicaceae; Calystegine; Functional divergence; Short chain dehydrogenase; Tropane alkaloid; Tropinone reductase

Indexed keywords

3-TROPINONE; ALCOHOL DEHYDROGENASE; TROPANE DERIVATIVE; TROPANONE; TROPINONE REDUCTASE; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 42549123527     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2008.03422.x     Document Type: Article
Times cited : (31)

References (55)
  • 1
    • 13244258549 scopus 로고    scopus 로고
    • Structure and reactivity of human mitochondrial 2,4-dienoyl-CoA reductase - Enzyme-ligand interactions in a distinctive short-chain reductase active site
    • Alphey, M.S., Yu, W.H., Byres, E., Li, D. Hunter, W.N. (2005) Structure and reactivity of human mitochondrial 2,4-dienoyl-CoA reductase - enzyme-ligand interactions in a distinctive short-chain reductase active site. J. Biol. Chem. 280, 3068 3077.
    • (2005) J. Biol. Chem. , vol.280 , pp. 3068-3077
    • Alphey, M.S.1    Yu, W.H.2    Byres, E.3    Li, D.4    Hunter, W.N.5
  • 3
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • Arabidopsis Genome Initiative (
    • Arabidopsis Genome Initiative (2000) Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature, 408, 796 815.
    • (2000) Nature , vol.408 , pp. 796-815
  • 4
    • 0034607947 scopus 로고    scopus 로고
    • Sugar-mimic glycosidase inhibitors: Natural occurrence, biological activity and prospects for therapeutic application
    • Asano, N., Nash, R.J., Molyneux, R.J. Fleet, G.W. (2000) Sugar-mimic glycosidase inhibitors: natural occurrence, biological activity and prospects for therapeutic application. Tetrahedron Asymmetry, 11, 1645 1680.
    • (2000) Tetrahedron Asymmetry , vol.11 , pp. 1645-1680
    • Asano, N.1    Nash, R.J.2    Molyneux, R.J.3    Fleet, G.W.4
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 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, 248 254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 20444397411 scopus 로고    scopus 로고
    • Calystegines in wild and cultivated Erythroxylum species
    • Brock, A., Bieri, S., Christen, P. Dräger, B. (2005) Calystegines in wild and cultivated Erythroxylum species. Phytochemistry, 66, 1231 1240.
    • (2005) Phytochemistry , vol.66 , pp. 1231-1240
    • Brock, A.1    Bieri, S.2    Christen, P.3    Dräger, B.4
  • 9
    • 20444446002 scopus 로고    scopus 로고
    • Monoterpene metabolism. Cloning, expression, and characterization of menthone reductases from peppermint
    • Davis, E.M., Ringer, K.L., McConkey, M.E. Croteau, R. (2005) Monoterpene metabolism. Cloning, expression, and characterization of menthone reductases from peppermint. Plant Physiol. 137, 873 881.
    • (2005) Plant Physiol. , vol.137 , pp. 873-881
    • Davis, E.M.1    Ringer, K.L.2    McConkey, M.E.3    Croteau, R.4
  • 10
    • 0037195484 scopus 로고    scopus 로고
    • Analysis of tropane and related alkaloids
    • Dräger, B. (2002) Analysis of tropane and related alkaloids. J. Chromatogr. A, 978, 1 35.
    • (2002) J. Chromatogr. a , vol.978 , pp. 1-35
    • Dräger, B.1
  • 11
    • 31344443596 scopus 로고    scopus 로고
    • Tropinone reductases, enzymes at the branch point of tropane alkaloid metabolism
    • Dräger, B. (2006) Tropinone reductases, enzymes at the branch point of tropane alkaloid metabolism. Phytochemistry, 67, 327 337.
    • (2006) Phytochemistry , vol.67 , pp. 327-337
    • Dräger, B.1
  • 12
    • 0001078463 scopus 로고
    • Levels of tropinone-reductase activities influence the spectrum of tropane esters found in transformed root cultures of Datura stramonium L
    • Dräger, B., Portsteffen, A., Schaal, A., MacCabe, P.H., Peerless, A.-C.J. Robins, R.J. (1992) Levels of tropinone-reductase activities influence the spectrum of tropane esters found in transformed root cultures of Datura stramonium L. Planta, 188, 581 586.
    • (1992) Planta , vol.188 , pp. 581-586
    • Dräger, B.1    Portsteffen, A.2    Schaal, A.3    MacCabe, P.H.4    Peerless, A.-C.J.5    Robins, R.J.6
  • 14
    • 0014276538 scopus 로고
    • Nutrient requirements of suspension cultures of soybean root cells
    • Gamborg, O.L., Miller, R.A. Ojima, K. (1968) Nutrient requirements of suspension cultures of soybean root cells. Exp. Cell Res. 50, 151 158.
    • (1968) Exp. Cell Res. , vol.50 , pp. 151-158
    • Gamborg, O.L.1    Miller, R.A.2    Ojima, K.3
  • 16
    • 27544456832 scopus 로고    scopus 로고
    • Complete reannotation of the Arabidopsis genome: Methods, tools, protocols and the final release
    • Haas, B.J., Wortman, J.R., Ronning, C.M. et al. (2005) Complete reannotation of the Arabidopsis genome: methods, tools, protocols and the final release. BMC Biol. 3, 7.
    • (2005) BMC Biol. , vol.3 , pp. 7
    • Haas, B.J.1    Wortman, J.R.2    Ronning, C.M.3
  • 17
    • 0001741417 scopus 로고
    • Two tropinone reductases with distinct stereospecificities from cultured roots of Hyoscyamus niger
    • Hashimoto, T., Nakajima, K., Ongena, G. Yamada, Y. (1992) Two tropinone reductases with distinct stereospecificities from cultured roots of Hyoscyamus niger. Plant Physiol. 100, 836 845.
    • (1992) Plant Physiol. , vol.100 , pp. 836-845
    • Hashimoto, T.1    Nakajima, K.2    Ongena, G.3    Yamada, Y.4
  • 18
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff, S. Henikoff, J.G. (1992) Amino acid substitution matrices from protein blocks. Proc. Natl Acad. Sci. USA, 89, 10915 10919.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 19
    • 0027317580 scopus 로고
    • Performance evaluation of amino acid substitution matrices
    • Henikoff, S. Henikoff, J.G. (1993) Performance evaluation of amino acid substitution matrices. Proteins, 17, 49 61.
    • (1993) Proteins , vol.17 , pp. 49-61
    • Henikoff, S.1    Henikoff, J.G.2
  • 20
    • 0017771466 scopus 로고
    • Evolution and tinkering
    • Jacob, F. (1977) Evolution and tinkering. Science, 196, 1161 1166.
    • (1977) Science , vol.196 , pp. 1161-1166
    • Jacob, F.1
  • 21
    • 0026380997 scopus 로고
    • On the evolution of plant secondary chemical diversity
    • Jones, C.G. Firn, R.D. (1991) On the evolution of plant secondary chemical diversity. Philos. Trans. R Soc. Lond. B, 333, 273 280.
    • (1991) Philos. Trans. R Soc. Lond. B , vol.333 , pp. 273-280
    • Jones, C.G.1    Firn, R.D.2
  • 22
    • 0029444383 scopus 로고
    • A genetic algorithm for flexible molecular overlay and pharmacophore elucidation
    • Jones, G., Willett, P. Glen, R.C. (1995) A genetic algorithm for flexible molecular overlay and pharmacophore elucidation. J. Comput. Aided Mol. Design, 9, 532 549.
    • (1995) J. Comput. Aided Mol. Design , vol.9 , pp. 532-549
    • Jones, G.1    Willett, P.2    Glen, R.C.3
  • 23
    • 33750990234 scopus 로고    scopus 로고
    • Immunolocalisation of two tropinone reductases in potato (Solanum tuberosum L.) root, stolon, and tuber sprouts
    • Kaiser, H., Richter, U., Keiner, R., Brabant, A., Hause, B. Drager, B. (2006) Immunolocalisation of two tropinone reductases in potato (Solanum tuberosum L.) root, stolon, and tuber sprouts. Planta, 225, 127 137.
    • (2006) Planta , vol.225 , pp. 127-137
    • Kaiser, H.1    Richter, U.2    Keiner, R.3    Brabant, A.4    Hause, B.5    Drager, B.6
  • 24
    • 33644766172 scopus 로고    scopus 로고
    • Prediction of coenzyme specificity in dehydrogenases/reductases - A hidden Markov model-based method and its application on complete genomes
    • Kallberg, Y. Persson, B. (2006) Prediction of coenzyme specificity in dehydrogenases/reductases - a hidden Markov model-based method and its application on complete genomes. FEBS J. 273, 1177 1184.
    • (2006) FEBS J. , vol.273 , pp. 1177-1184
    • Kallberg, Y.1    Persson, B.2
  • 25
    • 0342680025 scopus 로고    scopus 로고
    • Calystegine distribution in potato (Solanum tuberosum) tubers and plants
    • Keiner, R. Dräger, B. (2000) Calystegine distribution in potato (Solanum tuberosum) tubers and plants. Plant Sci. 150, 171 179.
    • (2000) Plant Sci. , vol.150 , pp. 171-179
    • Keiner, R.1    Dräger, B.2
  • 26
    • 0036007728 scopus 로고    scopus 로고
    • Molecular cloning, expression and characterization of tropinone reductase II, an enzyme of the SDR family in Solanum tuberosum (L.)
    • Keiner, R., Kaiser, H., Nakajima, K., Hashimoto, T. Dräger, B. (2002) Molecular cloning, expression and characterization of tropinone reductase II, an enzyme of the SDR family in Solanum tuberosum (L.). Plant Mol. Biol. 48, 299 308.
    • (2002) Plant Mol. Biol. , vol.48 , pp. 299-308
    • Keiner, R.1    Kaiser, H.2    Nakajima, K.3    Hashimoto, T.4    Dräger, B.5
  • 28
    • 2442445180 scopus 로고    scopus 로고
    • The variability of sesquiterpenes emitted from two Zea mays cultivars is controlled by allelic variation of two terpene synthase genes encoding stereoselective multiple product enzymes
    • Koellner, T.G., Schnee, C., Gershenzon, J. Degenhardt, J. (2004) The variability of sesquiterpenes emitted from two Zea mays cultivars is controlled by allelic variation of two terpene synthase genes encoding stereoselective multiple product enzymes. Plant Cell, 16, 1115 1131.
    • (2004) Plant Cell , vol.16 , pp. 1115-1131
    • Koellner, T.G.1    Schnee, C.2    Gershenzon, J.3    Degenhardt, J.4
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680 685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. Thornton, J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283 291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 31
    • 0006349639 scopus 로고
    • Biosynthesis of tropane alkaloids. 12. Biosynthesis of cochlearine
    • Liebisch, H.W., Bernasch, H. Schuette, H.R. (1973) Biosynthesis of tropane alkaloids. 12. Biosynthesis of cochlearine. Z. Chem. 13, 372 373.
    • (1973) Z. Chem. , vol.13 , pp. 372-373
    • Liebisch, H.W.1    Bernasch, H.2    Schuette, H.R.3
  • 32
    • 33947216707 scopus 로고    scopus 로고
    • Structural and biochemical characterization of human orphan DHRS10 reveals a novel cytosolic enzyme with steroid dehydrogenase activity
    • Lukacik, P., Keller, B., Bunkoczi, G., Kavanagh, K., Lee, W.H., Adamski, J. Oppermann, U. (2007) Structural and biochemical characterization of human orphan DHRS10 reveals a novel cytosolic enzyme with steroid dehydrogenase activity. Biochem. J. 402, 419 427.
    • (2007) Biochem. J. , vol.402 , pp. 419-427
    • Lukacik, P.1    Keller, B.2    Bunkoczi, G.3    Kavanagh, K.4    Lee, W.H.5    Adamski, J.6    Oppermann, U.7
  • 33
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell, A.D., Bashford, D., Bellott, M. et al. (1998) All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B, 102, 3586 3616.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586-3616
    • MacKerell, A.D.1    Bashford, D.2    Bellott, M.3
  • 34
    • 0027449067 scopus 로고
    • Two tropinone reductases with different stereospecificities are short-chain dehydrogenases evolved from a common ancestor
    • Nakajima, K., Hashimoto, T. Yamada, Y. (1993) Two tropinone reductases with different stereospecificities are short-chain dehydrogenases evolved from a common ancestor. Proc. Natl Acad. Sci. USA, 90, 9591 9595.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9591-9595
    • Nakajima, K.1    Hashimoto, T.2    Yamada, Y.3
  • 36
    • 0033523086 scopus 로고    scopus 로고
    • Site-directed mutagenesis of putative substrate-binding residues reveals a mechanism controlling the different stereospecificities of two tropinone reductases
    • Nakajima, K., Kato, H., Oda, J., Yamada, Y. Hashimoto, T. (1999a) Site-directed mutagenesis of putative substrate-binding residues reveals a mechanism controlling the different stereospecificities of two tropinone reductases. J. Biol. Chem. 274, 16563 16568.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16563-16568
    • Nakajima, K.1    Kato, H.2    Oda, J.3    Yamada, Y.4    Hashimoto, T.5
  • 39
    • 34547124814 scopus 로고    scopus 로고
    • Folate salvage in plants: Pterin aldehyde reduction is mediated by multiple non-specific aldehyde reductases
    • Noiriel, A., Naponelli, V., Bozzo, G.G., Gregory, J.F. III. Hanson, A.D. (2007) Folate salvage in plants: pterin aldehyde reduction is mediated by multiple non-specific aldehyde reductases. Plant J. 51, 378 389.
    • (2007) Plant J. , vol.51 , pp. 378-389
    • Noiriel, A.1    Naponelli, V.2    Bozzo, G.G.3    Gregory Iii., J.F.4    Hanson, A.D.5
  • 40
    • 12744267344 scopus 로고    scopus 로고
    • Short-chain dehydrogenases/reductases (SDR): The 2002 update
    • Oppermann, U., Filling, C., Hult, M. et al. (2003) Short-chain dehydrogenases/reductases (SDR): the 2002 update. Chem. Biol. Interact. 143/144, 247 253.
    • (2003) Chem. Biol. Interact. , vol.143-144 , pp. 247-253
    • Oppermann, U.1    Filling, C.2    Hult, M.3
  • 41
    • 0037149093 scopus 로고    scopus 로고
    • A generalized-born solvation model for macromolecular hybrid-potential calculations
    • Pellegrini, E. Field, M.J. (2002) A generalized-born solvation model for macromolecular hybrid-potential calculations. J. Phys. Chem. A, 106, 1316 1326.
    • (2002) J. Phys. Chem. a , vol.106 , pp. 1316-1326
    • Pellegrini, E.1    Field, M.J.2
  • 42
    • 32444433426 scopus 로고    scopus 로고
    • Biosynthesis of plant volatiles: Nature's diversity and ingenuity
    • Pichersky, E., Noel, J.P. Dudareva, N. (2006) Biosynthesis of plant volatiles: nature's diversity and ingenuity. Science, 311, 808 811.
    • (2006) Science , vol.311 , pp. 808-811
    • Pichersky, E.1    Noel, J.P.2    Dudareva, N.3
  • 44
    • 0028500354 scopus 로고
    • The reduction of tropinone in Datura stramonium root cultures by two specific reductases
    • Portsteffen, A., Dräger, B. Nahrstedt, A. (1994) The reduction of tropinone in Datura stramonium root cultures by two specific reductases. Phytochemistry, 37, 391 400.
    • (1994) Phytochemistry , vol.37 , pp. 391-400
    • Portsteffen, A.1    Dräger, B.2    Nahrstedt, A.3
  • 45
    • 33748761950 scopus 로고    scopus 로고
    • Molecular and enzymatic characterizations of novel bifunctional 3-beta-hydroxysteroid dehydrogenases/C-4 decarboxylases from Arabidopsis thaliana
    • Rahier, A., Darnet, S., Bouvier, F., Camara, B. Bard, M. (2006) Molecular and enzymatic characterizations of novel bifunctional 3-beta-hydroxysteroid dehydrogenases/C-4 decarboxylases from Arabidopsis thaliana. J. Biol. Chem. 281, 27264 27277.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27264-27277
    • Rahier, A.1    Darnet, S.2    Bouvier, F.3    Camara, B.4    Bard, M.5
  • 46
    • 16644387127 scopus 로고    scopus 로고
    • Repeated evolution of the pyrrolizidine alkaloid-mediated defense system in separate angiosperm lineages
    • Reimann, A., Nurhayati, N., Backenkoehler, A. Ober, D. (2004) Repeated evolution of the pyrrolizidine alkaloid-mediated defense system in separate angiosperm lineages. Plant Cell, 16, 2772 2784.
    • (2004) Plant Cell , vol.16 , pp. 2772-2784
    • Reimann, A.1    Nurhayati, N.2    Backenkoehler, A.3    Ober, D.4
  • 47
    • 0000618794 scopus 로고
    • Differential gene expression during somatic embryogenesis in Digitalis lanata analyzed by in vivo and in vitro protein synthesis
    • Reinbothe, C., Tewes, A., Luckner, M. Reinbothe, S. (1992) Differential gene expression during somatic embryogenesis in Digitalis lanata analyzed by in vivo and in vitro protein synthesis. Plant J. 2, 917 926.
    • (1992) Plant J. , vol.2 , pp. 917-926
    • Reinbothe, C.1    Tewes, A.2    Luckner, M.3    Reinbothe, S.4
  • 48
    • 0037249498 scopus 로고    scopus 로고
    • The Arabidopsis Information Resource (TAIR): A model organism database providing a centralized, curated gateway to Arabidopsis biology, research materials and community
    • Rhee, S.Y., Beavis, W., Berardini, T.Z. et al. (2003) The Arabidopsis Information Resource (TAIR): a model organism database providing a centralized, curated gateway to Arabidopsis biology, research materials and community. Nucleic Acids Res. 31, 224 228.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 224-228
    • Rhee, S.Y.1    Beavis, W.2    Berardini, T.Z.3
  • 49
    • 34247351552 scopus 로고    scopus 로고
    • Crystal structure of vestitone reductase from alfalfa (Medicago sativa L.)
    • Shao, H., Dixon, R.A. Wang, X.Q. (2007) Crystal structure of vestitone reductase from alfalfa (Medicago sativa L.). J. Mol. Biol. 369, 265 276.
    • (2007) J. Mol. Biol. , vol.369 , pp. 265-276
    • Shao, H.1    Dixon, R.A.2    Wang, X.Q.3
  • 50
    • 0025341310 scopus 로고
    • Calculation of conformational ensembles from potentials of mean force - An approach to the knowledge-based prediction of local structures in globular-proteins
    • Sippl, M.J. (1990) Calculation of conformational ensembles from potentials of mean force - an approach to the knowledge-based prediction of local structures in globular-proteins. J. Mol. Biol. 213, 859 883.
    • (1990) J. Mol. Biol. , vol.213 , pp. 859-883
    • Sippl, M.J.1
  • 52
    • 0036022960 scopus 로고    scopus 로고
    • Further development and validation of empirical scoring functions for structure-based binding affinity prediction
    • Wang, R., Lai, L. Wang, S. (2002) Further development and validation of empirical scoring functions for structure-based binding affinity prediction. J. Comput. Aided Mol. Design, 16, 11 26.
    • (2002) J. Comput. Aided Mol. Design , vol.16 , pp. 11-26
    • Wang, R.1    Lai, L.2    Wang, S.3
  • 53
    • 33847008037 scopus 로고    scopus 로고
    • Biochemical characterization of TASSELSEED 2, an essential plant short-chain dehydrogenase/reductase with broad spectrum activities
    • Wu, X.Q., Knapp, S., Stamp, A., Stammers, D.K., Jornvall, H., Dellaporta, S.L. Oppermann, U. (2007) Biochemical characterization of TASSELSEED 2, an essential plant short-chain dehydrogenase/reductase with broad spectrum activities. FEBS J. 274, 1172 1182.
    • (2007) FEBS J. , vol.274 , pp. 1172-1182
    • Wu, X.Q.1    Knapp, S.2    Stamp, A.3    Stammers, D.K.4    Jornvall, H.5    Dellaporta, S.L.6    Oppermann, U.7
  • 54
    • 0037953003 scopus 로고    scopus 로고
    • Capturing enzyme structure prior to reaction initiation: Tropinone reductase-II-substrate complexes
    • Yamashita, A., Endo, M., Higashi, T., Nakatsu, T., Yamada, Y., Oda, J. Kato, H. (2003) Capturing enzyme structure prior to reaction initiation: tropinone reductase-II-substrate complexes. Biochemistry, 42, 5566 5573.
    • (2003) Biochemistry , vol.42 , pp. 5566-5573
    • Yamashita, A.1    Endo, M.2    Higashi, T.3    Nakatsu, T.4    Yamada, Y.5    Oda, J.6    Kato, H.7
  • 55
    • 33749241876 scopus 로고    scopus 로고
    • Comparative transcript and alkaloid profiling in Papaver species identifies a short chain dehydrogenase/reductase involved in morphine biosynthesis
    • The EMBL accession number for the nucleotide sequence of Cotr is.
    • Ziegler, J., Voigtlander, S., Schmidt, J., Kramell, R., Miersch, O., Ammer, C., Gesell, A. Kutchan, T.M. (2006) Comparative transcript and alkaloid profiling in Papaver species identifies a short chain dehydrogenase/reductase involved in morphine biosynthesis. Plant J. 48, 177 192.
    • (2006) Plant J. , vol.48 , pp. 177-192
    • Ziegler, J.1    Voigtlander, S.2    Schmidt, J.3    Kramell, R.4    Miersch, O.5    Ammer, C.6    Gesell, A.7    Kutchan, T.M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.