메뉴 건너뛰기




Volumn 4, Issue JUL, 2013, Pages

Evolution of the key alkaloid enzyme putrescine N-methyltransferase from spermidine synthase

Author keywords

Arabidopsis thaliana; Datura stramonium; Evolution; Homology modeling; Putrescine N methyltransferase; Spermidine synthase

Indexed keywords


EID: 84900789620     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2013.00260     Document Type: Article
Times cited : (31)

References (53)
  • 2
    • 79956222409 scopus 로고    scopus 로고
    • Polyamine metabolic canalization in response to drought stress in Arabidopsis and the resurrection plant Craterostigma plantagineum
    • doi: 10.4161/psb.6.2.14317
    • Alcazar, R., Bitrian, M., Bartels, D., Koncz, C., Altabella, T., and Tiburcio, A. F. (2011). Polyamine metabolic canalization in response to drought stress in Arabidopsis and the resurrection plant Craterostigma plantagineum. Plant Signal. Behav. 6, 243-250. doi: 10.4161/psb.6.2.14317
    • (2011) Plant Signal. Behav. , vol.6 , pp. 243-250
    • Alcazar, R.1    Bitrian, M.2    Bartels, D.3    Koncz, C.4    Altabella, T.5    Tiburcio, A.F.6
  • 3
    • 0032493349 scopus 로고    scopus 로고
    • Jasmonate-induced responses are costly but benefit plants under attack in native populations
    • doi: 10.1073/pnas.95.14.8113
    • Baldwin, I. T. (1998). Jasmonate-induced responses are costly but benefit plants under attack in native populations. Proc. Natl. Acad. Sci. U.S.A. 95, 8113-8118. doi: 10.1073/pnas.95.14.8113
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 8113-8118
    • Baldwin, I.T.1
  • 4
    • 0028906425 scopus 로고
    • The chemistry of defense: Theory and practice
    • doi: 10.1073/pnas.92.1.2
    • Berenbaum, M. R. (1995). The chemistry of defense: theory and practice. Proc. Natl. Acad. Sci. U.S.A. 92, 2-8. doi: 10.1073/pnas.92.1.2
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 2-8
    • Berenbaum, M.R.1
  • 6
    • 70350729438 scopus 로고    scopus 로고
    • Putrescine N-methyltransferase-the start for alkaloids
    • doi: 10.1016/j.phytochem.2009.06.012
    • Biastoff, S., Brandt, W., and Draeger, B. (2009a). Putrescine N-methyltransferase-the start for alkaloids. Phytochemistry 70, 1708-1718. doi: 10.1016/j.phytochem.2009.06.012
    • (2009) Phytochemistry , vol.70 , pp. 1708-1718
    • Biastoff, S.1    Brandt, W.2    Draeger, B.3
  • 7
    • 70349883921 scopus 로고    scopus 로고
    • Evolution of putrescine N-methyltransferase from spermidine synthase demanded alterations in substrate binding
    • doi: 10.1016/j.febslet.2009.09.043
    • Biastoff, S., Reinhardt, N., Reva, V., Brandt, W., and Drager, B. (2009b). Evolution of putrescine N-methyltransferase from spermidine synthase demanded alterations in substrate binding. FEBS Lett. 583, 3367-3374. doi: 10.1016/j.febslet.2009.09.043
    • (2009) FEBS Lett. , vol.583 , pp. 3367-3374
    • Biastoff, S.1    Reinhardt, N.2    Reva, V.3    Brandt, W.4    Drager, B.5
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • doi: 10.1016/0003-2697(76)90527-3
    • 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. doi: 10.1016/0003-2697(76)90527-3
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 33748085361 scopus 로고    scopus 로고
    • Brassicaceae contain nortropane alkaloids
    • doi: 10.1016/j.phytochem.2006.06.024
    • Brock, A., Herzfeld, T., Paschke, R., Koch, M., and Drager, B. (2006). Brassicaceae contain nortropane alkaloids. Phytochemistry 67, 2050-2057. doi: 10.1016/j.phytochem.2006.06.024
    • (2006) Phytochemistry , vol.67 , pp. 2050-2057
    • Brock, A.1    Herzfeld, T.2    Paschke, R.3    Koch, M.4    Drager, B.5
  • 10
    • 78649529379 scopus 로고    scopus 로고
    • Crystal structures of NodS N-methyltransferase from Bradyrhizobium japonicum in ligand-free form and as SAH complex
    • doi: 10.1016/j.jmb.2010.10.016
    • Cakici, O., Sikorski, M., Stepkowski, T., Bujacz, G., and Jaskolski, M. (2010). Crystal structures of NodS N-methyltransferase from Bradyrhizobium japonicum in ligand-free form and as SAH complex. J. Mol. Biol. 404, 874-889. doi: 10.1016/j.jmb.2010.10.016
    • (2010) J. Mol. Biol. , vol.404 , pp. 874-889
    • Cakici, O.1    Sikorski, M.2    Stepkowski, T.3    Bujacz, G.4    Jaskolski, M.5
  • 12
    • 0242663237 scopus 로고    scopus 로고
    • A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations
    • doi: 10.1002/jcc.10349
    • Duan, Y., Wu, C., Chowdhury, S., Lee, M. C., Xiong, G., Zhang, W., et al. (2003). A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations. J. Comput. Chem. 24, 1999-2012. doi: 10.1002/jcc.10349
    • (2003) J. Comput. Chem. , vol.24 , pp. 1999-2012
    • Duan, Y.1    Wu, C.2    Chowdhury, S.3    Lee, M.C.4    Xiong, G.5    Zhang, W.6
  • 13
    • 34548587312 scopus 로고    scopus 로고
    • Crystal structure of Plasmodium falciparum spermidine synthase in complex with the substrate decarboxylated S-adenosylmethionine and the potent inhibitors 4MCHA and AdoDATO
    • doi: 10.1016/j.jmb.2007.07.053
    • Dufe, V. T., Qiu, W., Muller, I. B., Hui, R., Walter, R. D., and Al Karadaghi, S. (2007). Crystal structure of Plasmodium falciparum spermidine synthase in complex with the substrate decarboxylated S-adenosylmethionine and the potent inhibitors 4MCHA and AdoDATO. J. Mol. Biol. 373, 167-177. doi: 10.1016/j.jmb.2007.07.053
    • (2007) J. Mol. Biol. , vol.373 , pp. 167-177
    • Dufe, V.T.1    Qiu, W.2    Muller, I.B.3    Hui, R.4    Walter, R.D.5    Al Karadaghi, S.6
  • 14
    • 67650915748 scopus 로고    scopus 로고
    • Gene duplication and evolutionary novelty in plants
    • doi: 10.1111/j.1469-8137.2009.02923.x
    • Flagel, L. E., and Wendel, J. F. (2009). Gene duplication and evolutionary novelty in plants. New Phytol. 183, 557-564. doi: 10.1111/j.1469-8137.2009.02923.x
    • (2009) New Phytol. , vol.183 , pp. 557-564
    • Flagel, L.E.1    Wendel, J.F.2
  • 15
    • 0031881362 scopus 로고    scopus 로고
    • Molecular cloning of plant spermidine synthases
    • doi: 10.1093/oxfordjournals.pcp.a029291
    • Hashimoto, T., Tamaki, K., Suzuki, K., and Yamada, Y. (1998a). Molecular cloning of plant spermidine synthases. Plant Cell Physiol. 39, 73-79. doi: 10.1093/oxfordjournals.pcp.a029291
    • (1998) Plant Cell Physiol. , vol.39 , pp. 73-79
    • Hashimoto, T.1    Tamaki, K.2    Suzuki, K.3    Yamada, Y.4
  • 16
    • 0032080948 scopus 로고    scopus 로고
    • Intraspecific variability of the tandem repeats in Nicotiana putrescine N-methyltransferases
    • doi: 10.1023/A:1005961122814
    • Hashimoto, T., Shoji, T., Mihara, T., Oguri, H., Tamaki, K., Suzuki, K., et al. (1998b). Intraspecific variability of the tandem repeats in Nicotiana putrescine N-methyltransferases. Plant Mol. Biol. 37, 25-37. doi: 10.1023/A:1005961122814
    • (1998) Plant Mol. Biol. , vol.37 , pp. 25-37
    • Hashimoto, T.1    Shoji, T.2    Mihara, T.3    Oguri, H.4    Tamaki, K.5    Suzuki, K.6
  • 17
    • 25144443484 scopus 로고    scopus 로고
    • Structural basis for inhibition of histamine N-methyltransferase by diverse drugs
    • doi: 10.1016/j.jmb.2005.08.040
    • Horton, J. R., Sawada, K., Nishibori, M., and Cheng, X. (2005). Structural basis for inhibition of histamine N-methyltransferase by diverse drugs. J. Mol. Biol. 353, 334-344. doi: 10.1016/j.jmb.2005.08.040
    • (2005) J. Mol. Biol. , vol.353 , pp. 334-344
    • Horton, J.R.1    Sawada, K.2    Nishibori, M.3    Cheng, X.4
  • 18
    • 32944472945 scopus 로고    scopus 로고
    • Aminopropyltransferases: Function, structure and genetics
    • doi: 10.1093/jb/mvj019
    • Ikeguchi, Y., Bewley, M. C., and Pegg, A. E. (2006). Aminopropyltransferases: function, structure and genetics. J. Biochem. 139, 1-9. doi: 10.1093/jb/mvj019
    • (2006) J. Biochem. , vol.139 , pp. 1-9
    • Ikeguchi, Y.1    Bewley, M.C.2    Pegg, A.E.3
  • 19
    • 75549087305 scopus 로고    scopus 로고
    • The evolution of gene duplications: Classifying and distinguishing between models
    • doi: 10.1038/nrg2689
    • Innan, H., and Kondrashov, F. (2010). The evolution of gene duplications: classifying and distinguishing between models. Nat. Rev. Genet. 11, 97-108. doi: 10.1038/nrg2689
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 97-108
    • Innan, H.1    Kondrashov, F.2
  • 20
    • 77953623874 scopus 로고    scopus 로고
    • Enzyme promiscuity: A mechanistic and evolutionary perspective
    • doi: 10.1146/annurev-biochem-030409-143718
    • Khersonsky, O., and Tawfik, D. S. (2010). Enzyme promiscuity: a mechanistic and evolutionary perspective. Annu. Rev. Biochem. 79, 471-505. doi: 10.1146/annurev-biochem-030409-143718
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 471-505
    • Khersonsky, O.1    Tawfik, D.S.2
  • 21
    • 0036142291 scopus 로고    scopus 로고
    • The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor
    • doi: 10.1038/nsb737
    • Korolev, S., Ikeguchi, Y., Skarina, T., Beasley, S., Arrowsmith, C., Edwards, A., et al. (2002). The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor. Nat. Struct. Biol. 9, 27-31. doi: 10.1038/nsb737
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 27-31
    • Korolev, S.1    Ikeguchi, Y.2    Skarina, T.3    Beasley, S.4    Arrowsmith, C.5    Edwards, A.6
  • 22
    • 27844530636 scopus 로고    scopus 로고
    • Natural history of S-adenosylmethionine-binding proteins
    • doi: 10.1186/1472-6807-5-19
    • Kozbial, P. Z., and Mushegian, A. R. (2005). Natural history of S-adenosylmethionine-binding proteins. BMC Struct. Biol. 5:19. doi: 10.1186/1472-6807-5-19
    • (2005) BMC Struct. Biol. , vol.5 , pp. 19
    • Kozbial, P.Z.1    Mushegian, A.R.2
  • 23
    • 74249090260 scopus 로고    scopus 로고
    • Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling: Four approaches that performed well in CASP8
    • doi: 10.1002/prot.22570
    • Krieger, E., Joo, K., Lee, J., Lee, J., Raman, S., Thompson, J., et al. (2009). Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling: four approaches that performed well in CASP8. Proteins 77(Suppl. 9), 114-122. doi: 10.1002/prot.22570
    • (2009) Proteins , vol.77 , Issue.SUPPL. 9 , pp. 114-122
    • Krieger, E.1    Joo, K.2    Lee, J.3    Lee, J.4    Raman, S.5    Thompson, J.6
  • 24
    • 0037093644 scopus 로고    scopus 로고
    • Increasing the precision of comparative models with YASARA NOVA-a self-parameterizing force field
    • doi: 10.1002/prot.10104
    • Krieger, E., Koraimann, G., and Vriend, G. (2002). Increasing the precision of comparative models with YASARA NOVA-a self-parameterizing force field. Proteins 47, 393-402. doi: 10.1002/prot.10104
    • (2002) Proteins , vol.47 , pp. 393-402
    • Krieger, E.1    Koraimann, G.2    Vriend, G.3
  • 26
    • 0000243829 scopus 로고
    • Procheck-a program to check the stereochemical quality of protein structures
    • doi: 10.1107/S0021889892009944
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993). Procheck-a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291. doi: 10.1107/S0021889892009944
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    McArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 27
    • 0008349462 scopus 로고
    • Biosynthesis of shihunine in Dendrobium pierardii
    • doi: 10.1021/ja00436a042
    • Leete, E., and Bodem, G. B. (1976). Biosynthesis of shihunine in Dendrobium pierardii. J. Am. Chem. Soc. 98, 6321-6325. doi: 10.1021/ja00436a042
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 6321-6325
    • Leete, E.1    Bodem, G.B.2
  • 28
    • 34548387498 scopus 로고    scopus 로고
    • Ensemble refinement of protein crystal structures: Validation and application
    • doi: 10.1016/j.str.2007.06.019
    • Levin, E. J., Kondrashov, D. A., Wesenberg, G. E., and Phillips, G. N. Jr. (2007). Ensemble refinement of protein crystal structures: validation and application. Structure 15, 1040-1052. doi: 10.1016/j.str.2007.06.019
    • (2007) Structure , vol.15 , pp. 1040-1052
    • Levin, E.J.1    Kondrashov, D.A.2    Wesenberg, G.E.3    Phillips Jr., G.N.4
  • 29
    • 84979978581 scopus 로고
    • The tropane alkaloids
    • in, ed A. Brossi (New York, NY: Academic press)
    • Lounasmaa, M., and Tamminen, T. (1993). "The tropane alkaloids, " in The Alkaloids, ed A. Brossi (New York, NY: Academic press), 1-114.
    • (1993) The Alkaloids , pp. 1-114
    • Lounasmaa, M.1    Tamminen, T.2
  • 30
    • 0037990593 scopus 로고
    • Studies on Orchidaceae alkaloids III. The alkaloids in Dendrobium primulinumand Dendrobium chrysanthum
    • doi: 10.3891/acta.chem.scand.19-1607
    • Luening, B., and Leander, K. (1965). Studies on Orchidaceae alkaloids III. The alkaloids in Dendrobium primulinumand Dendrobium chrysanthum. Acta Chem. Scand. 19, 1607-1611. doi: 10.3891/acta.chem.scand.19-1607
    • (1965) Acta Chem. Scand. , vol.19 , pp. 1607-1611
    • Luening, B.1    Leander, K.2
  • 31
    • 0028965842 scopus 로고
    • Rapid high-performance liquid chromatographic method for the quantitation of polyamines as their dansyl derivatives: Application to plant and animal tissues
    • doi: 10.1016/0378-4347(94)00586-T
    • Marce, M., Brown, D. S., Capell, T., Figueras, X., and Tiburcio, A. F. (1995). Rapid high-performance liquid chromatographic method for the quantitation of polyamines as their dansyl derivatives: application to plant and animal tissues. J. Chromatogr. B Biomed. Appl. 666, 329-335. doi: 10.1016/0378-4347(94)00586-T
    • (1995) J. Chromatogr. B Biomed. Appl. , vol.666 , pp. 329-335
    • Marce, M.1    Brown, D.S.2    Capell, T.3    Figueras, X.4    Tiburcio, A.F.5
  • 32
    • 34250630530 scopus 로고    scopus 로고
    • The structure of two N-methyltransferases from the caffeine biosynthetic pathway
    • doi: 10.1104/pp.106.094854
    • McCarthy, A. A., and McCarthy, J. G. (2007). The structure of two N-methyltransferases from the caffeine biosynthetic pathway. Plant Physiol. 144, 879-889. doi: 10.1104/pp.106.094854
    • (2007) Plant Physiol. , vol.144 , pp. 879-889
    • McCarthy, A.A.1    McCarthy, J.G.2
  • 33
    • 52449127981 scopus 로고    scopus 로고
    • Evolutionary diversification in polyamine biosynthesis
    • doi: 10.1093/molbev/msn161
    • Minguet, E. G., Vera-Sirera, F., Marina, A., Carbonell, J., and Blazquez, M. A. (2008). Evolutionary diversification in polyamine biosynthesis. Mol. Biol. Evol. 25, 2119-2128. doi: 10.1093/molbev/msn161
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 2119-2128
    • Minguet, E.G.1    Vera-Sirera, F.2    Marina, A.3    Carbonell, J.4    Blazquez, M.A.5
  • 35
    • 77955935755 scopus 로고    scopus 로고
    • Gene duplications and the time thereafter-examples from plant secondary metabolism
    • Ober, D. (2010). Gene duplications and the time thereafter-examples from plant secondary metabolism. Plant Biol. (Stuttg.) 12, 570-577.
    • (2010) Plant Biol. (Stuttg.) , vol.12 , pp. 570-577
    • Ober, D.1
  • 37
    • 80052428125 scopus 로고    scopus 로고
    • Structural basis of substrate recognition in human nicotinamide N-methyltransferase
    • doi: 10.1021/bi2007614
    • Peng, Y., Sartini, D., Pozzi, V., Wilk, D., Emanuelli, M., and Yee, V. C. (2011). Structural basis of substrate recognition in human nicotinamide N-methyltransferase. Biochemistry 50, 7800-7808. doi: 10.1021/bi2007614
    • (2011) Biochemistry , vol.50 , pp. 7800-7808
    • Peng, Y.1    Sartini, D.2    Pozzi, V.3    Wilk, D.4    Emanuelli, M.5    Yee, V.C.6
  • 38
    • 0000647003 scopus 로고
    • Die Struktur des mesembrins und Mesembrenins
    • doi: 10.1007/BF00602769
    • Popelak, A., Lettenbauer, G., Haack, E., and Spingler, H. (1960). Die Struktur des mesembrins und Mesembrenins. Naturwissenschaften 47, 231-232. doi: 10.1007/BF00602769
    • (1960) Naturwissenschaften , vol.47 , pp. 231-232
    • Popelak, A.1    Lettenbauer, G.2    Haack, E.3    Spingler, H.4
  • 39
    • 0033911844 scopus 로고    scopus 로고
    • Evolutionary ecology of the tropane alkaloids of Datura stramonium L. (Solanaceae)
    • Shonle, I., and Bergelson, J. (2000). Evolutionary ecology of the tropane alkaloids of Datura stramonium L. (Solanaceae). Evolution 54, 778-788.
    • (2000) Evolution , vol.54 , pp. 778-788
    • Shonle, I.1    Bergelson, J.2
  • 40
    • 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
    • doi: 10.1016/S0022-2836(05)80269-4
    • 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. doi: 10.1016/S0022-2836(05)80269-4
    • (1990) J. Mol. Biol. , vol.213 , pp. 859-883
    • Sippl, M.J.1
  • 41
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • doi: 10.1002/prot.340170404
    • Sippl, M. J. (1993). Recognition of errors in three-dimensional structures of proteins. Proteins 17, 355-362. doi: 10.1002/prot.340170404
    • (1993) Proteins , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 42
    • 0001920296 scopus 로고
    • Separation and quantitation of polyamines in plant tissue by high performance liquid chromatography of their dansyl derivatives
    • doi: 10.1104/pp.78.1.89
    • Smith, M. A., and Davies, P. J. (1985). Separation and quantitation of polyamines in plant tissue by high performance liquid chromatography of their dansyl derivatives. Plant Physiol. 78, 89-91. doi: 10.1104/pp.78.1.89
    • (1985) Plant Physiol. , vol.78 , pp. 89-91
    • Smith, M.A.1    Davies, P.J.2
  • 43
    • 29444432259 scopus 로고    scopus 로고
    • Putrescine N-methyltransferase in Solanum tuberosum L., a calystegine-forming plant
    • doi: 10.1007/s00425-005-0077-z
    • Stenzel, O., Teuber, M., and Dräger, B. (2006). Putrescine N-methyltransferase in Solanum tuberosum L., a calystegine-forming plant. Planta 223, 200-212. doi: 10.1007/s00425-005-0077-z
    • (2006) Planta , vol.223 , pp. 200-212
    • Stenzel, O.1    Teuber, M.2    Dräger, B.3
  • 44
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • doi: 10.1093/molbev/msr121
    • Tamura, K., Peterson, D., Peterson, N., Stecher, G., Nei, M., and Kumar, S. (2011). MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol. Biol. Evol. 28, 2731-2739. doi: 10.1093/molbev/msr121
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 45
    • 33947137673 scopus 로고    scopus 로고
    • Putrescine N-methyltransferases-a structure-function analysis
    • doi: 10.1007/s11103-006-9126-7
    • Teuber, M., Azemi, M. E., Namjoyan, F., Meier, A. C., Wodak, A., Brandt, W., et al. (2007). Putrescine N-methyltransferases-a structure-function analysis. Plant Mol. Biol. 63, 787-801. doi: 10.1007/s11103-006-9126-7
    • (2007) Plant Mol. Biol. , vol.63 , pp. 787-801
    • Teuber, M.1    Azemi, M.E.2    Namjoyan, F.3    Meier, A.C.4    Wodak, A.5    Brandt, W.6
  • 46
    • 66649132872 scopus 로고    scopus 로고
    • Chaperonin overexpression promotes genetic variation and enzyme evolution
    • doi: 10.1038/nature08009
    • Tokuriki, N., and Tawfik, D. S. (2009). Chaperonin overexpression promotes genetic variation and enzyme evolution. Nature 459, 668-673. doi: 10.1038/nature08009
    • (2009) Nature , vol.459 , pp. 668-673
    • Tokuriki, N.1    Tawfik, D.S.2
  • 47
    • 84862996527 scopus 로고    scopus 로고
    • The rise of chemodiversity in plants
    • doi: 10.1126/science.1217411
    • Weng, J. K., Philippe, R. N., and Noel, J. P. (2012). The rise of chemodiversity in plants. Science 336, 1667-1670. doi: 10.1126/science.1217411
    • (2012) Science , vol.336 , pp. 1667-1670
    • Weng, J.K.1    Philippe, R.N.2    Noel, J.P.3
  • 48
    • 34447554595 scopus 로고    scopus 로고
    • Structure and mechanism of spermidine synthases
    • doi: 10.1021/bi602498k
    • Wu, H., Min, J. R., Ikeguchi, Y., Zeng, H., Dong, A. P., Loppnau, P., et al. (2007). Structure and mechanism of spermidine synthases. Biochemistry 46, 8331-8339. doi: 10.1021/bi602498k
    • (2007) Biochemistry , vol.46 , pp. 8331-8339
    • Wu, H.1    Min, J.R.2    Ikeguchi, Y.3    Zeng, H.4    Dong, A.P.5    Loppnau, P.6
  • 49
    • 0034679591 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of protein arginine methyltransferase PRMT3
    • doi: 10.1093/emboj/19.14.3509
    • Zhang, X., Zhou, L., and Cheng, X. (2000). Crystal structure of the conserved core of protein arginine methyltransferase PRMT3. EMBO J. 19, 3509-3519. doi: 10.1093/emboj/19.14.3509
    • (2000) EMBO J. , vol.19 , pp. 3509-3519
    • Zhang, X.1    Zhou, L.2    Cheng, X.3
  • 50
    • 76749130093 scopus 로고    scopus 로고
    • The crystal structure of Escherichia coli spermidine synthase SpeE reveals a unique substrate-binding pocket
    • doi: 10.1016/j.jsb.2009.12.024
    • Zhou, X. D., Chua, T. K., Tkaczuk, K. L., Bujnicki, J. M., and Sivaraman, J. (2010). The crystal structure of Escherichia coli spermidine synthase SpeE reveals a unique substrate-binding pocket. J. Struct. Biol. 169, 277-285. doi: 10.1016/j.jsb.2009.12.024
    • (2010) J. Struct. Biol. , vol.169 , pp. 277-285
    • Zhou, X.D.1    Chua, T.K.2    Tkaczuk, K.L.3    Bujnicki, J.M.4    Sivaraman, J.5
  • 51
    • 70349225934 scopus 로고    scopus 로고
    • Evolutionary and expression signatures of pseudogenes in Arabidopsis and rice
    • doi: 10.1104/pp.109.140632
    • Zou, C., Lehti-Shiu, M. D., Thibaud-Nissen, F., Prakash, T., Buell, C. R., and Shiu, S. H. (2009). Evolutionary and expression signatures of pseudogenes in Arabidopsis and rice. Plant Physiol. 151, 3-15. doi: 10.1104/pp.109.140632
    • (2009) Plant Physiol. , vol.151 , pp. 3-15
    • Zou, C.1    Lehti-Shiu, M.D.2    Thibaud-Nissen, F.3    Prakash, T.4    Buell, C.R.5    Shiu, S.H.6
  • 52
    • 0035119588 scopus 로고    scopus 로고
    • Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases
    • doi: 10.1038/85029
    • Zubieta, C., He, X. Z., Dixon, R. A., and Noel, J. P. (2001). Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases. Nat. Struct. Biol. 8, 271-279. doi: 10.1038/85029
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 271-279
    • Zubieta, C.1    He, X.Z.2    Dixon, R.A.3    Noel, J.P.4
  • 53
    • 0035983842 scopus 로고    scopus 로고
    • Structural basis for the modulation of lignin monomer methylation by caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase
    • doi: 10.1105/tpc.001412
    • Zubieta, C., Kota, P., Ferrer, J. L., Dixon, R. A., and Noel, J. P. (2002). Structural basis for the modulation of lignin monomer methylation by caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase. Plant Cell 14, 1265-1277. doi: 10.1105/tpc.001412
    • (2002) Plant Cell , vol.14 , pp. 1265-1277
    • Zubieta, C.1    Kota, P.2    Ferrer, J.L.3    Dixon, R.A.4    Noel, J.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.