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Volumn 54, Issue 3, 2004, Pages 415-425

Tobacco Nectarin III is a bifunctional enzyme with monodehydroascorbate reductase and carbonic anhydrase activities

Author keywords

carbonic anhydrase; monodehydroascorbate reductase; nectar; nectary; Nicotiana; ovary

Indexed keywords

FLORAL ORGANS; NECTAR; SEQUENCE ANALYSIS;

EID: 3042835494     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:PLAN.0000036373.84579.13     Document Type: Article
Times cited : (49)

References (41)
  • 3
    • 0002640138 scopus 로고
    • A brief historical review of the chemistry of floral nectar
    • B. Bentley and T. Elias (Eds.), Columbia University Press, New York
    • Baker, H.G. and Baker, I. 1983. A brief historical review of the chemistry of floral nectar. In: B. Bentley and T. Elias (Eds.), The Biology of Nectaries. Columbia University Press, New York, pp. 126-152.
    • (1983) The Biology of Nectaries , pp. 126-152
    • Baker, H.G.1    Baker, I.2
  • 4
    • 0344019333 scopus 로고
    • Nectar
    • Beutler, R. 1935. Nectar. Bee World 24: 106-116, 128-136, 156-162.
    • (1935) Bee World , vol.24 , pp. 106-116
    • Beutler, R.1
  • 5
    • 1642561810 scopus 로고
    • Vitamins, including carotenoids, chlorophylls and biologically active quinones
    • E. Stahl (Ed.), Springer-Verlag, Berlin
    • Bolliger, H. and König, A. 1969. Vitamins, including carotenoids, chlorophylls and biologically active quinones. In: E. Stahl (Ed.), Thin-Layer Chromatography: A Laboratory Handbook. Springer-Verlag, Berlin, pp. 259-311.
    • (1969) Thin-Layer Chromatography: A Laboratory Handbook , pp. 259-311
    • Bolliger, H.1    König, A.2
  • 6
    • 0033197629 scopus 로고    scopus 로고
    • Nectarin I is a novel, soluble germin-like protein expressed in the nectar of Nicotiana sp.
    • Carter, C., Graham, R. and Thornburg, R.W. 1999. Nectarin I is a novel, soluble germin-like protein expressed in the nectar of Nicotiana sp. Plant. Mol. Biol. 41: 207-216.
    • (1999) Plant. Mol. Biol. , vol.41 , pp. 207-216
    • Carter, C.1    Graham, R.2    Thornburg, R.W.3
  • 7
    • 0034711245 scopus 로고    scopus 로고
    • Tobacco Nectarin I: Purification and characterization as a germin-like, manganese superoxide dismutase implicated in the defense of floral reproductive tissues
    • Carter, C. and Thornburg, R.W. 2000. Tobacco Nectarin I: purification and characterization as a germin-like, manganese superoxide dismutase implicated in the defense of floral reproductive tissues. J. Biol. Cliem. 275: 36726-36733.
    • (2000) J. Biol. Cliem. , vol.275 , pp. 36726-36733
    • Carter, C.1    Thornburg, R.W.2
  • 8
    • 0037339667 scopus 로고    scopus 로고
    • The nectary-specific pattern of gene expression is regulated by multiple promoter elements in the tobacco Nectarin I promoter
    • Carter, C. and Thornburg, R.W. 2003. The nectary-specific pattern of gene expression is regulated by multiple promoter elements in the tobacco Nectarin I promoter. Plant Mol. Biol. 51: 451-457.
    • (2003) Plant Mol. Biol. , vol.51 , pp. 451-457
    • Carter, C.1    Thornburg, R.W.2
  • 9
    • 0842264011 scopus 로고    scopus 로고
    • Nectarin V is a flavin-containing berberine bridge enzyme-like protein with glucose oxidase activity
    • Carter, C.J. and Thornburg, R.W. 2004. Nectarin V is a flavin-containing berberine bridge enzyme-like protein with glucose oxidase activity. Plant Physiol. 134: 460-469.
    • (2004) Plant Physiol. , vol.134 , pp. 460-469
    • Carter, C.J.1    Thornburg, R.W.2
  • 10
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenolchloroform extraction
    • Chomczynski, P. and Sacchi, N. 1987. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenolchloroform extraction. Anal. Biochem. 162: 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 11
    • 0032882552 scopus 로고    scopus 로고
    • Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes
    • Christianson, D.W. and Cox, J.D. 1999. Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes. Annu. Rev. Biochem. 68: 33-57.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 33-57
    • Christianson, D.W.1    Cox, J.D.2
  • 12
    • 0029310607 scopus 로고
    • Isolation and characterisation of cDNA clones representing the genes encoding the major tuber storage protein (dioscorin) of yam (Dioscorea cayenensis Lam.)
    • Conlan, R.S., Griffiths, L.A., Napier, J.A., Shewry, P.R., Mantell, S. and Ainsworth, C. 1995. Isolation and characterisation of cDNA clones representing the genes encoding the major tuber storage protein (dioscorin) of yam (Dioscorea cayenensis Lam.). Plant Mol. Biol. 28: 369-380.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 369-380
    • Conlan, R.S.1    Griffiths, L.A.2    Napier, J.A.3    Shewry, P.R.4    Mantell, S.5    Ainsworth, C.6
  • 13
    • 84907126443 scopus 로고
    • Visualization of carbonic anhydrase activity in polyacrylamide gels
    • Edwards, L. and Patton, R. 1966. Visualization of carbonic anhydrase activity in polyacrylamide gels. Stain Tech 41: 333-334.
    • (1966) Stain Tech , vol.41 , pp. 333-334
    • Edwards, L.1    Patton, R.2
  • 15
    • 0001588680 scopus 로고
    • Über den enzymatischen Zuckerumbau in Nektarien
    • Frey-Wyssling, A., Zimmermann, M. and Maurizio, A. 1954. Über den enzymatischen Zuckerumbau in Nektarien. Experientia 10: 490-492.
    • (1954) Experientia , vol.10 , pp. 490-492
    • Frey-Wyssling, A.1    Zimmermann, M.2    Maurizio, A.3
  • 16
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling
    • Guex, N. and Peitsch, M.C. 1997. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modelling. Electrophoresis 18: 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 18
    • 0037895692 scopus 로고
    • Analysis of cations in nectars by means of a laser microprobe mass analyser (LAMMA)
    • Heinrich, G. 1989. Analysis of cations in nectars by means of a laser microprobe mass analyser (LAMMA). Beitr. Biol. Pflanz. 64: 293-308.
    • (1989) Beitr. Biol. Pflanz. , vol.64 , pp. 293-308
    • Heinrich, G.1
  • 19
    • 0033521146 scopus 로고    scopus 로고
    • Dioscorins, the major tuber storage proteins of yam (Dioscorea batatas Decne), with dehydroascorbate reductase and monodehydroascorbate reductase activities
    • Hou, W., Chen, H. and Lin, Y. 1999a. Dioscorins, the major tuber storage proteins of yam (Dioscorea batatas Decne), with dehydroascorbate reductase and monodehydroascorbate reductase activities. Plant Sci. 149: 151-156.
    • (1999) Plant Sci. , vol.149 , pp. 151-156
    • Hou, W.1    Chen, H.2    Lin, Y.3
  • 20
    • 0032841621 scopus 로고    scopus 로고
    • Dioscorin, the major tuber storage protein of yam (Dioscorea batatas Decne) with carbonic anhydrase and trypsin inhibitor activities
    • Hou, W., Liu, J., Chen, H., Chen, T., Chang, C. and Lin, Y. 1999b. Dioscorin, the major tuber storage protein of yam (Dioscorea batatas Decne) with carbonic anhydrase and trypsin inhibitor activities. J. Agric. Food Chem. 5: 2168-2172.
    • (1999) J. Agric. Food Chem. , vol.5 , pp. 2168-2172
    • Hou, W.1    Liu, J.2    Chen, H.3    Chen, T.4    Chang, C.5    Lin, Y.6
  • 21
    • 0034780180 scopus 로고    scopus 로고
    • Antioxidant activities of dioscorin, the storage protein of yam (Dioscorea batatas Decne) tuber
    • Hou, W.C., Lee, M.H., Chen, H.J., Liang, W.L., Han, C.H., Liu, Y.W. and Lin, Y.H. 2001. Antioxidant activities of dioscorin, the storage protein of yam (Dioscorea batatas Decne) tuber. J. Agric. Food Chem. 49: 4956-4960.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 4956-4960
    • Hou, W.C.1    Lee, M.H.2    Chen, H.J.3    Liang, W.L.4    Han, C.H.5    Liu, Y.W.6    Lin, Y.H.7
  • 22
    • 0032538339 scopus 로고    scopus 로고
    • Crystal structure of carbonic anhydrase from Neisseria gonorrhoeae and its complex with the inhibitor acetazolamide
    • Huang, S., Xue, Y., Sauer-Eriksson, E., Chirica, L., Lindskog, S. and Jonsson, B. 1998. Crystal structure of carbonic anhydrase from Neisseria gonorrhoeae and its complex with the inhibitor acetazolamide. J. Mol. Biol. 283: 301-310.
    • (1998) J. Mol. Biol. , vol.283 , pp. 301-310
    • Huang, S.1    Xue, Y.2    Sauer-Eriksson, E.3    Chirica, L.4    Lindskog, S.5    Jonsson, B.6
  • 24
    • 0001277128 scopus 로고
    • Electrophoresis of red cell NADH- And NADPH-diaphorases in normal subjects and patients with congenital methemoglobinemia
    • Kaplan, J. and Beutler, E. 1967. Electrophoresis of red cell NADH- and NADPH-diaphorases in normal subjects and patients with congenital methemoglobinemia. Biochem. Biophys. Res. Comm. 29: 605-610.
    • (1967) Biochem. Biophys. Res. Comm. , vol.29 , pp. 605-610
    • Kaplan, J.1    Beutler, E.2
  • 25
    • 2142677666 scopus 로고
    • Different temporal and spatial gene expression patterns occur during anther development
    • Koltunow, A.M., Truettner, J., Cox, K.H., Walroth, M. and Goldberg, R.B. 1990. Different temporal and spatial gene expression patterns occur during anther development. Plant Cell 2: 1201-1224.
    • (1990) Plant Cell , vol.2 , pp. 1201-1224
    • Koltunow, A.M.1    Truettner, J.2    Cox, K.H.3    Walroth, M.4    Goldberg, R.B.5
  • 26
    • 3042622680 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of a 'lost' unstable flower color phenotype in interspecific crosses of Nicotiana sp.
    • Kornaga, T., Zyzak, D.V., Kintinar, A., Baynes, J. and Thornburg, R. 1997. Genetic and biochemical characterization of a 'lost' unstable flower color phenotype in interspecific crosses of Nicotiana sp. WWW J. Biol. 2: 8.
    • (1997) WWW J. Biol. , vol.2 , pp. 8
    • Kornaga, T.1    Zyzak, D.V.2    Kintinar, A.3    Baynes, J.4    Thornburg, R.5
  • 27
    • 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
  • 28
    • 0029111330 scopus 로고
    • Trypsin inhibitor and trypsin-like protease activity in air or submergence-grown rice (Oryza sativa L.) coleoptiles
    • Lee, T. and Lin, Y. 1995. Trypsin inhibitor and trypsin-like protease activity in air or submergence-grown rice (Oryza sativa L.) coleoptiles. Plant Sci. 106: 43-54.
    • (1995) Plant Sci. , vol.106 , pp. 43-54
    • Lee, T.1    Lin, Y.2
  • 29
    • 0027105007 scopus 로고
    • A knowledge base for predicting protein localization sites in eukaryotic cells
    • Nakai, K. and Kanehisa, M. 1992. A knowledge base for predicting protein localization sites in eukaryotic cells. Genomics 14: 897-911.
    • (1992) Genomics , vol.14 , pp. 897-911
    • Nakai, K.1    Kanehisa, M.2
  • 30
    • 0029004590 scopus 로고
    • Protein modeling by E-mail
    • Peitsch, M.C. 1995. Protein modeling by E-mail. Bio/Technology 13: 658-660.
    • (1995) Bio/Technology , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 31
    • 0030053370 scopus 로고    scopus 로고
    • ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling
    • Peitsch, M.C. 1996. ProMod and Swiss-Model: internet-based tools for automated comparative protein modelling. Biochem. Soc. Trans. 24: 274-279.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 274-279
    • Peitsch, M.C.1
  • 33
    • 0025374510 scopus 로고
    • Ascorbic acid metabolism in protection against free radicals: A radiation model
    • Rose, R. 1990. Ascorbic acid metabolism in protection against free radicals: a radiation model. Biochem. Biophys. Res. Commun. 169: 430-436.
    • (1990) Biochem. Biophys. Res. Commun. , vol.169 , pp. 430-436
    • Rose, R.1
  • 34
    • 0020560669 scopus 로고
    • Formation of hydroxyl radicals from hydrogen peroxide and iron salts by superoxide-and ascorbate-dependent mechanisms: Relevance to the pathology of rheumatoid disease
    • Lond.
    • Rowley, D. and Halliwell, B. 1983. Formation of hydroxyl radicals from hydrogen peroxide and iron salts by superoxide-and ascorbate-dependent mechanisms: relevance to the pathology of rheumatoid disease. Clin. Sci. (Lond.) 64: 649-653.
    • (1983) Clin. Sci. , vol.64 , pp. 649-653
    • Rowley, D.1    Halliwell, B.2
  • 35
    • 0024215145 scopus 로고
    • Ascorbate/iron mediation of hydroxyl free radical damage to PBR322 plasmid DNA
    • Schneider, J., Browning, M. and Floyd, R. 1988. Ascorbate/iron mediation of hydroxyl free radical damage to PBR322 plasmid DNA. Free Radic. Biol. Med. 5: 287-295.
    • (1988) Free Radic. Biol. Med. , vol.5 , pp. 287-295
    • Schneider, J.1    Browning, M.2    Floyd, R.3
  • 36
    • 0345431646 scopus 로고
    • Nectar constituents in the genus Fremontia (Sterculiaceae): Sugars, flavonoids and proteins
    • Scogin, R. 1979. Nectar constituents in the genus Fremontia (Sterculiaceae): sugars, flavonoids and proteins. Bot. Gaz. 140: 29-31.
    • (1979) Bot. Gaz. , vol.140 , pp. 29-31
    • Scogin, R.1
  • 38
    • 0035966050 scopus 로고    scopus 로고
    • Carbonic anhydrase: New insights for an ancient enzyme
    • Tripp, B.C., Smith, K. and Ferry, J.G. 2001. Carbonic anhydrase: new insights for an ancient enzyme. J. Biol. Chem. 276: 48615-48618.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48615-48618
    • Tripp, B.C.1    Smith, K.2    Ferry, J.G.3
  • 39
    • 0034129712 scopus 로고    scopus 로고
    • Proteomic study of the peripheral proteins from thylakoid membranes of the cyanobacterium Synechocystis sp. PCC6803
    • Wang, Y., Sun, J. and Chitnis, P. 2000. Proteomic study of the peripheral proteins from thylakoid membranes of the cyanobacterium Synechocystis sp. PCC6803. Electrophoresis 21: 1746-1754.
    • (2000) Electrophoresis , vol.21 , pp. 1746-1754
    • Wang, Y.1    Sun, J.2    Chitnis, P.3
  • 40
  • 41
    • 3042710914 scopus 로고
    • Papierchromatographische Untersuchungen über die pflanzliche Zuckersekretion
    • Zimmermann, M. 1953. Papierchromatographische Untersuchungen über die pflanzliche Zuckersekretion. Ber. Schweiz Botan. Ges. 63: 402-429.
    • (1953) Ber. Schweiz Botan. Ges. , vol.63 , pp. 402-429
    • Zimmermann, M.1


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