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Volumn 47, Issue 1, 1996, Pages 245-271

Dioxygenases: Molecular structure and role in plant metabolism

Author keywords

Alkaloid biosynthesis; Ethylene biosynthesis; Flavonoid biosynthesis; Gibberellin biosynthesis; Lipoxygenase

Indexed keywords


EID: 0000916977     PISSN: 10402519     EISSN: None     Source Type: Journal    
DOI: 10.1146/annurev.arplant.47.1.245     Document Type: Article
Times cited : (242)

References (169)
  • 4
    • 0027393905 scopus 로고
    • Isolation of a ripening and wound-induced cDNA from Cucumis melo L. encoding a protein with homology to the ethylene-forming enzyme
    • Balagué C, Watson CF, Turner AJ, Rouge P, Picton S, et al. 1993. Isolation of a ripening and wound-induced cDNA from Cucumis melo L. encoding a protein with homology to the ethylene-forming enzyme. Eur. J. Biochem. 212:27-34
    • (1993) Eur. J. Biochem. , vol.212 , pp. 27-34
    • Balagué, C.1    Watson, C.F.2    Turner, A.J.3    Rouge, P.4    Picton, S.5
  • 6
    • 0027759974 scopus 로고
    • Characterization of an Arabidopsis lipoxygenase gene responsive to methyl jasmonate and wounding
    • Bell E, Mullet JE. 1993. Characterization of an Arabidopsis lipoxygenase gene responsive to methyl jasmonate and wounding. Plant Physiol. 103:1133-37
    • (1993) Plant Physiol. , vol.103 , pp. 1133-1137
    • Bell, E.1    Mullet, J.E.2
  • 7
    • 0021096474 scopus 로고
    • γ-butyrobetaine hydroxylase: Primary and secondary tritium kinetic isotope effects
    • Blanchard JS, Englard S. 1983. γ-butyrobetaine hydroxylase: primary and secondary tritium kinetic isotope effects. Biochemistry 22:5922-29
    • (1983) Biochemistry , vol.22 , pp. 5922-5929
    • Blanchard, J.S.1    Englard, S.2
  • 8
    • 0020392390 scopus 로고
    • γ-butyrobetaine hydroxylase: A unique protective effect of catalase
    • Blanchard JS, Englard S, Kondo A. 1982. γ-butyrobetaine hydroxylase: a unique protective effect of catalase. Arch. Biochem. Biophys. 219:327-34
    • (1982) Arch. Biochem. Biophys. , vol.219 , pp. 327-334
    • Blanchard, J.S.1    Englard, S.2    Kondo, A.3
  • 10
    • 0022102924 scopus 로고
    • Elicitor-induced prolyl hydroxylase from French bean (Phaseolus vulgaris)
    • Bolwell GP, Robbins MP, Dixon RA. 1985. Elicitor-induced prolyl hydroxylase from French bean (Phaseolus vulgaris). Biochem. J. 229:693-99
    • (1985) Biochem. J. , vol.229 , pp. 693-699
    • Bolwell, G.P.1    Robbins, M.P.2    Dixon, R.A.3
  • 12
    • 1642558270 scopus 로고
    • Subcellular localization of the sites of conversion of 1-aminocyclopropane-1-carboxylic acid into ethylene in plant cells
    • Bouzayen M, Latché A, Pech JC. 1990. Subcellular localization of the sites of conversion of 1-aminocyclopropane-1-carboxylic acid into ethylene in plant cells. Planta 180:175-80
    • (1990) Planta , vol.180 , pp. 175-180
    • Bouzayen, M.1    Latché, A.2    Pech, J.C.3
  • 13
    • 0027246677 scopus 로고
    • The three-dimensional structure of an arachidonic acid 15-lipoxygenase
    • Boyington JC, Gaffney BJ, Amzel LM. 1993. The three-dimensional structure of an arachidonic acid 15-lipoxygenase. Science 260:1482-86
    • (1993) Science , vol.260 , pp. 1482-1486
    • Boyington, J.C.1    Gaffney, B.J.2    Amzel, L.M.3
  • 14
    • 0025042203 scopus 로고
    • Purification and characterization of flavone synthase I, a 2-oxoglutarate-dependent desaturase
    • Britsch L. 1990. Purification and characterization of flavone synthase I, a 2-oxoglutarate-dependent desaturase. Arch. Biochem. Biophys. 282:152-60
    • (1990) Arch. Biochem. Biophys. , vol.282 , pp. 152-160
    • Britsch, L.1
  • 15
    • 0025016915 scopus 로고
    • Purification of flavanone 3β-hydroxylase from Petunia hybrida: Antibody preparation and characterization of a chemogenetically defined mutant
    • Britsch L. 1990. Purification of flavanone 3β-hydroxylase from Petunia hybrida: antibody preparation and characterization of a chemogenetically defined mutant. Arch. Biochem. Biophys. 276:348-54
    • (1990) Arch. Biochem. Biophys. , vol.276 , pp. 348-354
    • Britsch, L.1
  • 16
  • 17
    • 0023040154 scopus 로고
    • Purification and characterization of (2S)-flavanone 3-hydroxylase from Petunia hybrida
    • Britsch L, Grisebach H. 1986. Purification and characterization of (2S)-flavanone 3-hydroxylase from Petunia hybrida. Eur. J. Biochem. 156:569-77
    • (1986) Eur. J. Biochem. , vol.156 , pp. 569-577
    • Britsch, L.1    Grisebach, H.2
  • 18
    • 0026646769 scopus 로고
    • Molecular cloning, sequence analysis, and in vitro expression of flavanone 3β-hydroxylase from Petunia hybrida
    • Britsch L, Ruhnau-Brich B, Forkmann G. 1992. Molecular cloning, sequence analysis, and in vitro expression of flavanone 3β-hydroxylase from Petunia hybrida. J. Biol. Chem. 267:5380-87
    • (1992) J. Biol. Chem. , vol.267 , pp. 5380-5387
    • Britsch, L.1    Ruhnau-Brich, B.2    Forkmann, G.3
  • 19
    • 77049164909 scopus 로고
    • Ascorbic acid in aromatic hydroxylation II. Products formed by reaction of substrates with ascorbic acid, ferrous ion, and oxygen
    • Brodie BB, Axelrod J, Shore PA, Udenfriend S. 1954. Ascorbic acid in aromatic hydroxylation II. Products formed by reaction of substrates with ascorbic acid, ferrous ion, and oxygen. J. Biol. Chem. 208: 741-50
    • (1954) J. Biol. Chem. , vol.208 , pp. 741-750
    • Brodie, B.B.1    Axelrod, J.2    Shore, P.A.3    Udenfriend, S.4
  • 20
    • 0022907609 scopus 로고
    • Absolute configuration of the hydroxyeicosatetraenoic acids (HTETEs) formed during catalytic oxygenation of ara chidonic acid by microsomal cytochrome P-450
    • Capdevila J, Yadagiri P, Manna S, Falck JR. 1986. Absolute configuration of the hydroxyeicosatetraenoic acids (HTETEs) formed during catalytic oxygenation of ara chidonic acid by microsomal cytochrome P-450. Biochem. Biophys. Res. Commun. 141:1007-11
    • (1986) Biochem. Biophys. Res. Commun. , vol.141 , pp. 1007-1011
    • Capdevila, J.1    Yadagiri, P.2    Manna, S.3    Falck, J.R.4
  • 21
  • 23
    • 0011387765 scopus 로고
    • Deguelin cyclase, a prenyl to chromen transforming enzyme from Tephrosia vogellii
    • Crombie L, Rossiter JT, Van Bruggen N, Whiting DA. 1992. Deguelin cyclase, a prenyl to chromen transforming enzyme from Tephrosia vogellii. Phytochemistry 31:451-61
    • (1992) Phytochemistry , vol.31 , pp. 451-461
    • Crombie, L.1    Rossiter, J.T.2    Van Bruggen, N.3    Whiting, D.A.4
  • 24
    • 0027689341 scopus 로고
    • A Malus cDNA with homology to the Antirrhinum Candica and Zea A2 genes
    • Davies KM. 1993. A Malus cDNA with homology to the Antirrhinum Candica and Zea A2 genes. Plant Physiol. 103:1015
    • (1993) Plant Physiol. , vol.103 , pp. 1015
    • Davies, K.M.1
  • 25
    • 0027537947 scopus 로고
    • Purification, characterization, and kinetic analysis of a 2-oxoglutarate-dependent dioxygenase involved in vindoline biosynthesis from Catharanthus roseus
    • De Carolis E, De Luca V. 1993. Purification, characterization, and kinetic analysis of a 2-oxoglutarate-dependent dioxygenase involved in vindoline biosynthesis from Catharanthus roseus. J. Biol. Chem. 268: 5504-11
    • (1993) J. Biol. Chem. , vol.268 , pp. 5504-5511
    • De Carolis, E.1    De Luca, V.2
  • 26
    • 0029294727 scopus 로고
    • Flavanone 3-hydroxylase transcripts and flavonol accumulation are temporally coordinate in maize anthers
    • Deboo GB, Albertsen MC, Taylor LP. 1995. Flavanone 3-hydroxylase transcripts and flavonol accumulation are temporally coordinate in maize anthers. Plant J. 7: 703-13
    • (1995) Plant J. , vol.7 , pp. 703-713
    • Deboo, G.B.1    Albertsen, M.C.2    Taylor, L.P.3
  • 27
    • 0001747592 scopus 로고
    • Molecular cloning of the flavanone 3β-hydroxylase gene (FHT) from carnation (Dianthus caryophyllus) and analysis of stable and unstable FHT mutants
    • Dedio J, Saedler H, Forkmann G. 1995. Molecular cloning of the flavanone 3β-hydroxylase gene (FHT) from carnation (Dianthus caryophyllus) and analysis of stable and unstable FHT mutants. Theor. Appl. Genet. 90:611-17
    • (1995) Theor. Appl. Genet. , vol.90 , pp. 611-617
    • Dedio, J.1    Saedler, H.2    Forkmann, G.3
  • 28
    • 0024118269 scopus 로고
    • Interaction of a DNA binding factor with the 5́-flanking region of an ethylene-responsive fruit ripening gene from tomato
    • Deikman J, Fischer RL. 1988. Interaction of a DNA binding factor with the 5́-flanking region of an ethylene-responsive fruit ripening gene from tomato. EMBO J. 7: 3315-20
    • (1988) EMBO J. , vol.7 , pp. 3315-3320
    • Deikman, J.1    Fischer, R.L.2
  • 29
    • 0026699542 scopus 로고
    • Purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from apple fruit
    • Dong JG, Fernández-Maculet JC, Yang SF. 1992. Purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from apple fruit. Proc. Natl. Acad. Sci. USA 89:9789-93
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9789-9793
    • Dong, J.G.1    Fernández-Maculet, J.C.2    Yang, S.F.3
  • 30
    • 0000397283 scopus 로고
    • Expression of ethylene biosynthetic pathway mRNAs is spatially regulated within carnation flower petals
    • Drory A, Mayak S, Woodson WR. 1993. Expression of ethylene biosynthetic pathway mRNAs is spatially regulated within carnation flower petals. J. Plant Physiol. 141:663-67
    • (1993) J. Plant Physiol. , vol.141 , pp. 663-667
    • Drory, A.1    Mayak, S.2    Woodson, W.R.3
  • 31
    • 0027357637 scopus 로고
    • Purification, properties and partial amino-acid sequence of 1-aminocyclopropane-1-carboxylic acid oxidase from apple fruits
    • Dupille E, Rombaldi C, Lelièvre J-M, Cleyet-Marel J-C, Pech JC, Latché A. 1993. Purification, properties and partial amino-acid sequence of 1-aminocyclopropane-1-carboxylic acid oxidase from apple fruits. Planta 190:65-70
    • (1993) Planta , vol.190 , pp. 65-70
    • Dupille, E.1    Rombaldi, C.2    Lelièvre, J.-M.3    Cleyet-Marel, J.-C.4    Pech, J.C.5    Latché, A.6
  • 32
    • 0028055816 scopus 로고
    • Complex spatial and temporal expression of lipoxygenase genes during Phaseolus vulgaris (L.) development
    • Eiben HG, Slusarenko AJ. 1994. Complex spatial and temporal expression of lipoxygenase genes during Phaseolus vulgaris (L.) development. Plant J. 5:123-35
    • (1994) Plant J. , vol.5 , pp. 123-135
    • Eiben, H.G.1    Slusarenko, A.J.2
  • 33
    • 0026486822 scopus 로고
    • Primary structure deduced from complementary DNA sequence and expression in cultured cells of mammalian 4-hydroxyphenylpyruvic acid dioxygenase
    • Endo F, Awata H, Tanoue A, Ishiguro M, Eda Y, et al. 1992. Primary structure deduced from complementary DNA sequence and expression in cultured cells of mammalian 4-hydroxyphenylpyruvic acid dioxygenase. J. biol. Chem. 267:24235-40
    • (1992) J. Biol. Chem. , vol.267 , pp. 24235-24240
    • Endo, F.1    Awata, H.2    Tanoue, A.3    Ishiguro, M.4    Eda, Y.5
  • 34
    • 0022459326 scopus 로고
    • The biochemical functions of ascorbic acid
    • Englard S, Seifter S. 1986. The biochemical functions of ascorbic acid. Annu. Rev. Nutr. 6:365-406
    • (1986) Annu. Rev. Nutr. , vol.6 , pp. 365-406
    • Englard, S.1    Seifter, S.2
  • 35
    • 0029132294 scopus 로고
    • Molecular characterisation of a gene encoding homogentisate dioxygenase from Aspergillus nidulans and identification of its human and plant homologues
    • Fernández-Cañón JM, Peñalva MA. 1995. Molecular characterisation of a gene encoding homogentisate dioxygenase from Aspergillus nidulans and identification of its human and plant homologues. J. Biol. Chem. 270:21199-205
    • (1995) J. Biol. Chem. , vol.270 , pp. 21199-21205
    • Fernández-Cañón, J.M.1    Peñalva, M.A.2
  • 37
    • 0028080656 scopus 로고
    • 2 on ACC oxidase activity from roots of sunflower (Helianthus annuus) seed-lings
    • 2 on ACC oxidase activity from roots of sunflower (Helianthus annuus) seed-lings. Photochemistry 35:847-51
    • (1994) Photochemistry , vol.35 , pp. 847-851
    • Finlayson, S.A.1    Reid, D.M.2
  • 38
    • 85053492389 scopus 로고
    • Ascorbic acid
    • ed. RG Alscher, JL Hess, Boca Raton: CRC
    • Foyer CH. 1993. Ascorbic acid. In Antioxidants in Higher Plants, ed. RG Alscher, JL Hess, pp. 31-58. Boca Raton: CRC
    • (1993) Antioxidants in Higher Plants , pp. 31-58
    • Foyer, C.H.1
  • 39
    • 0026485632 scopus 로고
    • Molecular cloning in Escherichia coli, expression, and nucleotide sequence of the gene for the ethylene-forming enzyme of Pseudomonas syringae pv. phaseolicola PK2
    • Fukuda H, Ogawa T, Ishihara K, Fujii T, Nagahama K, et al. 1992. Molecular cloning in Escherichia coli, expression, and nucleotide sequence of the gene for the ethylene-forming enzyme of Pseudomonas syringae pv. phaseolicola PK2. Biochem. Biophys. Res. Commun. 188: 826-32
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 826-832
    • Fukuda, H.1    Ogawa, T.2    Ishihara, K.3    Fujii, T.4    Nagahama, K.5
  • 41
    • 0027980155 scopus 로고
    • Heterologous expression of the gene for the ethylene-forming enzyme from Pseudomonas syringae in the cyanobacterium Synechococcus
    • Fukuda H, Sakai M, Nagahama K, Fujii T, Matsuoka M, et al. 1994. Heterologous expression of the gene for the ethylene-forming enzyme from Pseudomonas syringae in the cyanobacterium Synechococcus. Biotech. Lett. 16:1-6
    • (1994) Biotech. Lett. , vol.16 , pp. 1-6
    • Fukuda, H.1    Sakai, M.2    Nagahama, K.3    Fujii, T.4    Matsuoka, M.5
  • 43
    • 0025741241 scopus 로고
    • Recent investigations into the lipoxygenase pathway of plants
    • Gardner HW. 1991. Recent investigations into the lipoxygenase pathway of plants. Biochim. Biophys. Acta 1084:221-39
    • (1991) Biochim. Biophys. Acta , vol.1084 , pp. 221-239
    • Gardner, H.W.1
  • 44
    • 0002616342 scopus 로고
    • Partial purification of gibberellin oxidases from spinach leaves
    • Gilmour SJ, Bleecker AB, Zeevaart JAD. 1987. Partial purification of gibberellin oxidases from spinach leaves. Plant Physiol. 85:87-90
    • (1987) Plant Physiol. , vol.85 , pp. 87-90
    • Gilmour, S.J.1    Bleecker, A.B.2    Zeevaart, J.A.D.3
  • 45
    • 0001587467 scopus 로고
    • Gibberellin metabolism in cell-free extracts from spinach leaves in relation to photoperiod
    • Gilmour SJ, Zeevaart JAD, Schwenen L, Graebe JE. 1986. Gibberellin metabolism in cell-free extracts from spinach leaves in relation to photoperiod. Plant Physiol. 82: 190-95
    • (1986) Plant Physiol. , vol.82 , pp. 190-195
    • Gilmour, S.J.1    Zeevaart, J.A.D.2    Schwenen, L.3    Graebe, J.E.4
  • 46
    • 0001069705 scopus 로고
    • Gibberellin biosynthesis and control
    • Graebe JE. 1987. Gibberellin biosynthesis and control. Annu. Rev. Plant Physiol. 38: 419-65
    • (1987) Annu. Rev. Plant Physiol. , vol.38 , pp. 419-465
    • Graebe, J.E.1
  • 47
    • 0026861497 scopus 로고
    • Molecular biology of fruit ripening and its manipulation with antisense genes
    • Gray J, Picton S, Shabbeer J, Schuch W, Grierson D. 1992. Molecular biology of fruit ripening and its manipulation with antisense genes. Plant Mol. Biol 19:69-87
    • (1992) Plant Mol. Biol , vol.19 , pp. 69-87
    • Gray, J.1    Picton, S.2    Shabbeer, J.3    Schuch, W.4    Grierson, D.5
  • 48
    • 0001761639 scopus 로고
    • Partial purification of two gibberellin 2β-hydroxylases from cotyledons of Phaseolus vulgaris
    • Griggs DL, Hedden P, Lazarus CM. 1991. Partial purification of two gibberellin 2β-hydroxylases from cotyledons of Phaseolus vulgaris. Photochemistry 30: 2507-12
    • (1991) Photochemistry , vol.30 , pp. 2507-2512
    • Griggs, D.L.1    Hedden, P.2    Lazarus, C.M.3
  • 50
    • 0002238687 scopus 로고
    • Inhibition of ethylene production in sunflower cell suspensions by the plant growth retardant BAS 111., W: Possible relations to changes in polyamine and cytokinin contents
    • Grossmann K, Siefert F, Kwiatkowski J, Schraudner M, Langebartels C, Sandermann H Jr. 1993. Inhibition of ethylene production in sunflower cell suspensions by the plant growth retardant BAS 111., W: possible relations to changes in polyamine and cytokinin contents. J. Plant Growth Regul. 12:5-11
    • (1993) J. Plant Growth Regul. , vol.12 , pp. 5-11
    • Grossmann, K.1    Siefert, F.2    Kwiatkowski, J.3    Schraudner, M.4    Langebartels, C.5    Sandermann Jr., H.6
  • 51
    • 0025820641 scopus 로고
    • Identification of a tomato gene for the ethylene-forming enzyme by expression in yeast
    • Hamilton AJ, Bouzayen M, Grierson D. 1991. Identification of a tomato gene for the ethylene-forming enzyme by expression in yeast. Proc. Natl. Acad. Sci. USA 88:7434-37
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7434-7437
    • Hamilton, A.J.1    Bouzayen, M.2    Grierson, D.3
  • 52
    • 0001375191 scopus 로고
    • Antisense gene that inhibits synthesis of the hormone ethylene in transgenic plants
    • Hamilton AJ, Lycett GW, Grierson D. 1990. Antisense gene that inhibits synthesis of the hormone ethylene in transgenic plants. Nature 346:284-87
    • (1990) Nature , vol.346 , pp. 284-287
    • Hamilton, A.J.1    Lycett, G.W.2    Grierson, D.3
  • 53
    • 0029015335 scopus 로고
    • Mutations at the C-terminal isoleucine and other potential iron ligands of 5-lipoxygenase
    • Hammarberg T, Zhang Y-Y, Lind B, Rådmark O, Samuelsson B. 1995. Mutations at the C-terminal isoleucine and other potential iron ligands of 5-lipoxygenase. Eur. J. Biochem. 230:401-7
    • (1995) Eur. J. Biochem. , vol.230 , pp. 401-407
    • Hammarberg, T.1    Zhang, Y.-Y.2    Lind, B.3    Rådmark, O.4    Samuelsson, B.5
  • 54
    • 0025782677 scopus 로고
    • Hyoscyamine 6β-hydroxylase, an enzyme involved in tropane alkaloid biosynthesis, is located at the pericycle of the root
    • Hashimoto T, Hayashi A, Amano Y, Kohno J, Iwanari H, et al. 1991. Hyoscyamine 6β-hydroxylase, an enzyme involved in tropane alkaloid biosynthesis, is located at the pericycle of the root. J. Biol Chem. 266:4648-53
    • (1991) J. Biol Chem. , vol.266 , pp. 4648-4653
    • Hashimoto, T.1    Hayashi, A.2    Amano, Y.3    Kohno, J.4    Iwanari, H.5
  • 55
    • 0027248795 scopus 로고
    • Two-step epoxidation of hyoscyamine to scopolamine is catalyzed by bifunctional hyoscyamine 6β-hydroxylase
    • Hashimoto T, Matsuda J, Yamada Y. 1993. Two-step epoxidation of hyoscyamine to scopolamine is catalyzed by bifunctional hyoscyamine 6β-hydroxylase. FEBS Lett. 329:35-39
    • (1993) FEBS Lett. , vol.329 , pp. 35-39
    • Hashimoto, T.1    Matsuda, J.2    Yamada, Y.3
  • 56
    • 0023654599 scopus 로고
    • Purification and characterization of hyoscyamine 6β-hydroxylase from root cultures of Hyoscyamus niger L.
    • Hashimoto T, Yamada Y. 1987. Purification and characterization of hyoscyamine 6β-hydroxylase from root cultures of Hyoscyamus niger L. Eur. J. Biochem. 164: 277-85
    • (1987) Eur. J. Biochem. , vol.164 , pp. 277-285
    • Hashimoto, T.1    Yamada, Y.2
  • 58
    • 0000236964 scopus 로고
    • The biosynthesis of 12a-hydroxylated gibberellins in a cell-free system from Cucurbita maxima endosperm
    • Hedden P, Graebe JE, Beale MH, Gaskin P, MacMillan J. 1984. The biosynthesis of 12a-hydroxylated gibberellins in a cell-free system from Cucurbita maxima endosperm. Phytochemistry 23:569-74
    • (1984) Phytochemistry , vol.23 , pp. 569-574
    • Hedden, P.1    Graebe, J.E.2    Beale, M.H.3    Gaskin, P.4    MacMillan, J.5
  • 59
    • 0000155014 scopus 로고
    • Biosynthesis
    • ed. JB Harborne, London: Chapman & Hall
    • Heller W, Forkmann G. 1988. Biosynthesis. In The Flavonoids, ed. JB Harborne, pp. 399-425. London: Chapman & Hall
    • (1988) The Flavonoids , pp. 399-425
    • Heller, W.1    Forkmann, G.2
  • 60
    • 0002338138 scopus 로고
    • Organisation and expression of a wound/ripening-related small multigene family from tomato
    • Holdsworth MJ, Schuch W, Grierson D. 1988. Organisation and expression of a wound/ripening-related small multigene family from tomato. Plant Mol. Biol. 11: 81-88
    • (1988) Plant Mol. Biol. , vol.11 , pp. 81-88
    • Holdsworth, M.J.1    Schuch, W.2    Grierson, D.3
  • 61
    • 0027762788 scopus 로고
    • Cloning and expression of flavonol synthase from Petunia hybrida
    • Holton TA, Brugliera F, Tanaka Y. 1993. Cloning and expression of flavonol synthase from Petunia hybrida. Plant J. 4: 1003-10
    • (1993) Plant J. , vol.4 , pp. 1003-1010
    • Holton, T.A.1    Brugliera, F.2    Tanaka, Y.3
  • 62
    • 0028080557 scopus 로고
    • The role of ascorbate free radical as an electron acceptor to cytochrome b-mediated trans-plasma membrane electron transport in higher plants
    • Horemans N, Asard H, Caubergs RJ. 1994. The role of ascorbate free radical as an electron acceptor to cytochrome b-mediated trans-plasma membrane electron transport in higher plants. Plant Physiol. 104:1455-58
    • (1994) Plant Physiol. , vol.104 , pp. 1455-1458
    • Horemans, N.1    Asard, H.2    Caubergs, R.J.3
  • 63
    • 0026409862 scopus 로고
    • Perspectives on non-heme iron protein chemistry
    • Howard JB, Rees DC. 1991. Perspectives on non-heme iron protein chemistry. Adv. Protein Chem. 42:199-280
    • (1991) Adv. Protein Chem. , vol.42 , pp. 199-280
    • Howard, J.B.1    Rees, D.C.2
  • 64
    • 0001371475 scopus 로고
    • Characterization and induction of the activity of 1-aminocyclopropane-1-carboxylate oxidase in the wounded mesocarp tissue of Cucurbita maxima
    • Hyodo H, Hashimoto C, Morozumi S. Hu W, Tanaka K. 1993. Characterization and induction of the activity of 1-aminocyclopropane-1-carboxylate oxidase in the wounded mesocarp tissue of Cucurbita maxima. Plant Cell Physiol 34:667-71
    • (1993) Plant Cell Physiol , vol.34 , pp. 667-671
    • Hyodo, H.1    Hashimoto, C.2    Morozumi, S.3    Hu, W.4    Tanaka, K.5
  • 65
    • 0026578185 scopus 로고
    • Mutagenesis studies on the amino acid residues involved in the iron-binding and the activity of human 5-lipoxygenase
    • Ishii S, Noguchi M, Miyano M, Matsumoto T, Noma M. 1992. Mutagenesis studies on the amino acid residues involved in the iron-binding and the activity of human 5-lipoxygenase. Biochem. Biophys. Res. Commun. 182:1482-90
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 1482-1490
    • Ishii, S.1    Noguchi, M.2    Miyano, M.3    Matsumoto, T.4    Noma, M.5
  • 66
    • 0029141892 scopus 로고
    • Delayed leaf senescence in ethylene-deficient ACC-oxidase antisense tomato plants: Molecular and physiological analysis
    • John I, Drake R, Farrell A, Cooper W, Lee P, et al. 1995. Delayed leaf senescence in ethylene-deficient ACC-oxidase antisense tomato plants: molecular and physiological analysis. Plant J. 7:483-90
    • (1995) Plant J. , vol.7 , pp. 483-490
    • John, I.1    Drake, R.2    Farrell, A.3    Cooper, W.4    Lee, P.5
  • 67
    • 1842408475 scopus 로고
    • Oxidation of 1-aminocyclopropane-1-carboxylic acid (ACC) in the generation of ethylene by plants
    • ed. RM Wallsgrove, Cambridge: Cambridge Univ. Press
    • John P. 1995. Oxidation of 1-aminocyclopropane-1-carboxylic acid (ACC) in the generation of ethylene by plants. In Amino Acids and Their Derivatives in Higher Plants, ed. RM Wallsgrove, pp. 51-58. Cambridge: Cambridge Univ. Press
    • (1995) Amino Acids and Their Derivatives in Higher Plants , pp. 51-58
    • John, P.1
  • 68
    • 0001459408 scopus 로고
    • The biosynthesis of all major pea gibberellins in a cell-free system from Pisum sativum
    • Kamiya Y, Graebe JE. 1983. The biosynthesis of all major pea gibberellins in a cell-free system from Pisum sativum. Phytochemistry 22:681-89
    • (1983) Phytochemistry , vol.22 , pp. 681-689
    • Kamiya, Y.1    Graebe, J.E.2
  • 69
    • 7544220038 scopus 로고
    • Partial characterization of the gibberellin 3β-hydroxylase from immature seeds of Phaseolus vulgaris
    • ed. N Takahashi, BO Phinney, J MacMillan, New York: Springer-Verlag
    • Kamiya Y, Kwak S-S. 1990. Partial characterization of the gibberellin 3β-hydroxylase from immature seeds of Phaseolus vulgaris. In Gibberellins, ed. N Takahashi, BO Phinney, J MacMillan, pp. 72-81. New York: Springer-Verlag
    • (1990) Gibberellins , pp. 72-81
    • Kamiya, Y.1    Kwak, S.-S.2
  • 70
    • 0028445983 scopus 로고
    • Species-dependent expression of the hyoscyamine 6β-hydroxylase gene in the pericycle
    • Kanegae T, Kajiya H, Amano Y, Hashimoto T, Yamada Y. 1994. Species-dependent expression of the hyoscyamine 6β-hydroxylase gene in the pericycle. Plant Physiol. 105:483-90
    • (1994) Plant Physiol. , vol.105 , pp. 483-490
    • Kanegae, T.1    Kajiya, H.2    Amano, Y.3    Hashimoto, T.4    Yamada, Y.5
  • 72
    • 84989669781 scopus 로고
    • 14C of methionine into the mugineic acid family of phytosiderophores in iron-deficient barley roots
    • 14C of methionine into the mugineic acid family of phytosiderophores in iron-deficient barley roots. Physiol. Plant. 88:668-74
    • (1993) Physiol. Plant , vol.88 , pp. 668-674
    • Kawai, S.1    Itoh, K.2    Takagi, S.3
  • 74
    • 0028155462 scopus 로고
    • Structure and expression of cDNAs encoding 1-aminocyclopropane-1-carboxylate oxidase homologs isolated from excised mung bean hypocotyls
    • Kim WT, Yang SF. 1994. Structure and expression of cDNAs encoding 1-aminocyclopropane-1-carboxylate oxidase homologs isolated from excised mung bean hypocotyls. Planta 194:223-29
    • (1994) Planta , vol.194 , pp. 223-229
    • Kim, W.T.1    Yang, S.F.2
  • 75
    • 0000950271 scopus 로고
    • Mapping of ripening-related or -specific cDNAclones of tomato (Lycopersicon esculentum)
    • Kinzer SM, Schwager SJ, Mutschler MA. 1990. Mapping of ripening-related or -specific cDNAclones of tomato (Lycopersicon esculentum). Theor. Appl. Genet. 79: 489-96
    • (1990) Theor. Appl. Genet. , vol.79 , pp. 489-496
    • Kinzer, S.M.1    Schwager, S.J.2    Mutschler, M.A.3
  • 76
    • 0002079883 scopus 로고
    • Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins
    • ed. JJ Harding, MJC Crabbe. Boca Raton: CRC
    • Kivirikko KI, Myllylä R, Pihlajaniemi T. 1992. Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins. In Post-translational Modifications of Proteins, ed. JJ Harding, MJC Crabbe. pp. 1-51. Boca Raton: CRC
    • (1992) Post-translational Modifications of Proteins , pp. 1-51
    • Kivirikko, K.I.1    Myllylä, R.2    Pihlajaniemi, T.3
  • 77
    • 0028641345 scopus 로고
    • Position 713 is critical for catalysis but not iron binding in soybean lipoxygenase 3
    • Kramer JA, Johnson KR, Dunham WR, Sands RH, Funk MO Jr. 1994. Position 713 is critical for catalysis but not iron binding in soybean lipoxygenase 3. Biochemistry 33:15017-22
    • (1994) Biochemistry , vol.33 , pp. 15017-15022
    • Kramer, J.A.1    Johnson, K.R.2    Dunham, W.R.3    Sands, R.H.4    Funk Jr., M.O.5
  • 78
    • 0028928192 scopus 로고
    • Molecular cloning and heterologous expression of a cDNA encoding berbamunine synthase, a C-O phenol-coupling cytochrome P450 from the higher plant Berberis stolonifera
    • Kraus PFX. Kutchan TM. 1995. Molecular cloning and heterologous expression of a cDNA encoding berbamunine synthase, a C-O phenol-coupling cytochrome P450 from the higher plant Berberis stolonifera. Proc. Natl. Acad. Sci. USA 92: 2071-75
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2071-2075
    • Kraus, P.F.X.1    Kutchan, T.M.2
  • 79
    • 0006218968 scopus 로고
    • Modulation of ethylene synthesis in acotyledonous soybean and wheat seedlings
    • Kraus TE, Murr DP, Hofstra G, Fletcher RA. 1992. Modulation of ethylene synthesis in acotyledonous soybean and wheat seedlings. J. Plant Growth Regul. 11: 47-53
    • (1992) J. Plant Growth Regul. , vol.11 , pp. 47-53
    • Kraus, T.E.1    Murr, D.P.2    Hofstra, G.3    Fletcher, R.A.4
  • 80
    • 0000457448 scopus 로고
    • Partial purification and characterization of gibberellin 3β-hydroxylase from immature seeds of Phaseolus vulgaris L.
    • Kwak S-S, Kamiya Y, Sakurai A. Takahashi N, Graebe JE. 1988. Partial purification and characterization of gibberellin 3β-hydroxylase from immature seeds of Phaseolus vulgaris L. Plant Cell Physiol. 29:935-43
    • (1988) Plant Cell Physiol. , vol.29 , pp. 935-943
    • Kwak, S.-S.1    Kamiya, Y.2    Sakurai, A.3    Takahashi, N.4    Graebe, J.E.5
  • 81
    • 51249164053 scopus 로고
    • Biosynthesis of 12α- and 13-hydroxylated gibberellins in a cell-free system from Cucurbita maxima endosperm and the identification of new endogenous gibberellins
    • Lange T, Hedden P, Graebe JE. 1993. Biosynthesis of 12α- and 13-hydroxylated gibberellins in a cell-free system from Cucurbita maxima endosperm and the identification of new endogenous gibberellins. Planta 189:340-49
    • (1993) Planta , vol.189 , pp. 340-349
    • Lange, T.1    Hedden, P.2    Graebe, J.E.3
  • 82
    • 0028016322 scopus 로고
    • Expression cloning of a gibberellin 20-oxidase, a multifunctional enzyme involved in gibberellin biosynthesis
    • Lange T, Hedden P, Graebe JE. 1994. Expression cloning of a gibberellin 20-oxidase, a multifunctional enzyme involved in gibberellin biosynthesis. Proc. Natl. Acad. Sci. USA 91:8552-56
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8552-8556
    • Lange, T.1    Hedden, P.2    Graebe, J.E.3
  • 83
    • 0028188586 scopus 로고
    • Separation and characterisation of three 2-oxoglutarate-dependent dioxygenases from Cucurbita maxima L. endosperm involved in gibberellin biosynthesis
    • Lange T, Schweimer A, Ward DA, Hedden P, Graebe JE. 1994. Separation and characterisation of three 2-oxoglutarate-dependent dioxygenases from Cucurbita maxima L. endosperm involved in gibberellin biosynthesis. Planta 195:98-107
    • (1994) Planta , vol.195 , pp. 98-107
    • Lange, T.1    Schweimer, A.2    Ward, D.A.3    Hedden, P.4    Graebe, J.E.5
  • 85
    • 0011626793 scopus 로고
    • Concerning the presence and formation of ascorbic acid in yeasts
    • Leung CT, Loewus FA. 1985. Concerning the presence and formation of ascorbic acid in yeasts. Plant Sci. 38:65-69
    • (1985) Plant Sci. , vol.38 , pp. 65-69
    • Leung, C.T.1    Loewus, F.A.2
  • 86
    • 0023896637 scopus 로고
    • Diverse mechanisms for the regulation of ethyleneinducible gene expression
    • Lincoln JE, Fischer RL. 1988. Diverse mechanisms for the regulation of ethyleneinducible gene expression. Mol. Gen. Genet. 212:71-75
    • (1988) Mol. Gen. Genet. , vol.212 , pp. 71-75
    • Lincoln, J.E.1    Fischer, R.L.2
  • 87
    • 12044251152 scopus 로고
    • Role of ascorbate in detoxifying ozone in the apoplast of spinach (Spinacia oleracea L.) leaves
    • Luwe MWF, Takahama U, Heber U. 1993. Role of ascorbate in detoxifying ozone in the apoplast of spinach (Spinacia oleracea L.) leaves. Plant Physiol. 101: 969-76
    • (1993) Plant Physiol. , vol.101 , pp. 969-976
    • Luwe, M.W.F.1    Takahama, U.2    Heber, U.3
  • 88
    • 0001431019 scopus 로고
    • Two related biosynthetic pathways of mugineic acids in Gramineous plants
    • Ma JF, Nomoto K. 1993. Two related biosynthetic pathways of mugineic acids in Gramineous plants. Plant Physiol. 102: 373-78
    • (1993) Plant Physiol. , vol.102 , pp. 373-378
    • Ma, J.F.1    Nomoto, K.2
  • 90
    • 0027999314 scopus 로고
    • Lipoxygenase activity associated to isolated soybean plasma membranes
    • Macrì F, Braidot E, Petrussa E, Vianello A. 1994. Lipoxygenase activity associated to isolated soybean plasma membranes. Biochim. Biophys. Acta 1215:109-14
    • (1994) Biochim. Biophys. Acta , vol.1215 , pp. 109-114
    • Macrì, F.1    Braidot, E.2    Petrussa, E.3    Vianello, A.4
  • 91
  • 92
    • 0019510669 scopus 로고
    • An intramembranous reductant which participates in the proline hydroxylation reaction with intracisternal prolyl hydroxylase and unhydroxylated procollagen in isolated microsomes from L-929 cells
    • Mata JM, Assad R, Peterkofsky B. 1981. An intramembranous reductant which participates in the proline hydroxylation reaction with intracisternal prolyl hydroxylase and unhydroxylated procollagen in isolated microsomes from L-929 cells. Arch. Biochem. Biophys. 206:93-104
    • (1981) Arch. Biochem. Biophys. , vol.206 , pp. 93-104
    • Mata, J.M.1    Assad, R.2    Peterkofsky, B.3
  • 93
    • 0025786893 scopus 로고
    • Molecular cloning of hyoscyamine 6β-hydroxylase, a 2-oxoglutarate-dependent dioxygenase, from cultured roots of Hyoscyamus niger
    • Matsuda J. Okabe S, Hashimoto T, Yamada Y. 1991. Molecular cloning of hyoscyamine 6β-hydroxylase, a 2-oxoglutarate-dependent dioxygenase, from cultured roots of Hyoscyamus niger. J. Biol. Chem. 266:9460-64
    • (1991) J. Biol. Chem. , vol.266 , pp. 9460-9464
    • Matsuda, J.1    Okabe, S.2    Hashimoto, T.3    Yamada, Y.4
  • 94
    • 0026646836 scopus 로고
    • Characterization and kinetic parameters of ethylene-forming enzyme from avocado fruit
    • McGarvey DJ, Christoffersen RE. 1992. Characterization and kinetic parameters of ethylene-forming enzyme from avocado fruit. J. Biol. Chem. 267:5964-67
    • (1992) J. Biol. Chem. , vol.267 , pp. 5964-5967
    • McGarvey, D.J.1    Christoffersen, R.E.2
  • 95
    • 0010426793 scopus 로고
    • 2-facilitated conversion of 1-aminocyclopropane-1-carboxylic acid to ethylene in model systems and intact tissues
    • 2-facilitated conversion of 1-aminocyclopropane-1-carboxylic acid to ethylene in model systems and intact tissues. Plant Physiol 73:784-90
    • (1983) Plant Physiol , vol.73 , pp. 784-790
    • McRae, D.G.1    Coker, J.A.2    Legge, R.L.3    Thompson, J.E.4
  • 96
    • 0027539326 scopus 로고
    • An Arabidopsis thaliana lipoxygenase gene can be induced by pathogens, abscisic acid, and methyl jasmonate
    • Melan MA, Dong X, Endara ME, Davis KR, Ausubel FM, Peterman TK. 1993. An Arabidopsis thaliana lipoxygenase gene can be induced by pathogens, abscisic acid, and methyl jasmonate. Plant Physiol. 101: 441-50
    • (1993) Plant Physiol. , vol.101 , pp. 441-450
    • Melan, M.A.1    Dong, X.2    Endara, M.E.3    Davis, K.R.4    Ausubel, F.M.5    Peterman, T.K.6
  • 97
    • 0028011119 scopus 로고
    • Structure and sequence of the Arafcidopsis thaliana lipoxygenase 1 gene
    • Melan MA, Nemhauser JL, Peterman TK. 1994. Structure and sequence of the Arafcidopsis thaliana lipoxygenase 1 gene. Biochim. Biophys. Acta 1210:377-80
    • (1994) Biochim. Biophys. Acta , vol.1210 , pp. 377-380
    • Melan, M.A.1    Nemhauser, J.L.2    Peterman, T.K.3
  • 98
    • 0025074950 scopus 로고
    • The En/Spm transposable element of Zea mays contains splice sites at the termini generating a novel intron from a dSpm element in the A2 gene
    • Menssen A, Höhmann S, Martin W, Schnable PS, Peterson PA, et al. 1990. The En/Spm transposable element of Zea mays contains splice sites at the termini generating a novel intron from a dSpm element in the A2 gene. EMBO J. 9:3051-57
    • (1990) EMBO J. , vol.9 , pp. 3051-3057
    • Menssen, A.1    Höhmann, S.2    Martin, W.3    Schnable, P.S.4    Peterson, P.A.5
  • 99
    • 0027260861 scopus 로고
    • Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1
    • Minor W, Steczko J, Bolin JT, Otwinowski Z, Axelrod B. 1993. Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1. Biochemistry 32:6320-23
    • (1993) Biochemistry , vol.32 , pp. 6320-6323
    • Minor, W.1    Steczko, J.2    Bolin, J.T.3    Otwinowski, Z.4    Axelrod, B.5
  • 100
    • 0028830671 scopus 로고
    • 2-activated 1-aminocyclopropane-1-carboxylate oxidase activity from apple fruit
    • 2-activated 1-aminocyclopropane-1-carboxylate oxidase activity from apple fruit. Phytochemistry 39: 751-55
    • (1995) Phytochemistry , vol.39 , pp. 751-755
    • Mizutani, F.1    Dong, J.G.2    Yang, S.F.3
  • 101
    • 0028051112 scopus 로고
    • Activity of 1-aminocyclopropane-1-carboxylate (ACC) oxidase (ethylene-forming enzyme) in the pulp and peel of ripening bananas
    • Moya-León MA, John P. 1994. Activity of 1-aminocyclopropane-1-carboxylate (ACC) oxidase (ethylene-forming enzyme) in the pulp and peel of ripening bananas. J. Hort. Sci. 69:243-50
    • (1994) J. Hort. Sci. , vol.69 , pp. 243-250
    • Moya-León, M.A.1    John, P.2
  • 102
    • 0029141614 scopus 로고
    • Purification and biochemical characterization of 1-aminocyclopropane-1-carboxylate oxidase from banana fruit
    • Moya-Leon MA, John P. 1995. Purification and biochemical characterization of 1-aminocyclopropane-1-carboxylate oxidase from banana fruit. Phytochemistry 39: 15-20
    • (1995) Phytochemistry , vol.39 , pp. 15-20
    • Moya-Leon, M.A.1    John, P.2
  • 103
    • 0026656134 scopus 로고
    • Modification of vertebrate and algal prolyl 4-hydroxylases and vertebrate lysyl hydroxylase by diethyl pyrocarbonate
    • Myllylä R, Günzler V, Kivirikko KI, Kaska DD. 1992. Modification of vertebrate and algal prolyl 4-hydroxylases and vertebrate lysyl hydroxylase by diethyl pyrocarbonate. Biochem. J. 286:923-27
    • (1992) Biochem. J. , vol.286 , pp. 923-927
    • Myllylä, R.1    Günzler, V.2    Kivirikko, K.I.3    Kaska, D.D.4
  • 104
    • 0021329173 scopus 로고
    • Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase
    • Myllylä R, Majamaa K, Günzler V, Hanauske-Abel HM, Kivirikko KI. 1984. Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase. J. Biol. Chem. 259:5403-5
    • (1984) J. Biol. Chem. , vol.259 , pp. 5403-5405
    • Myllylä, R.1    Majamaa, K.2    Günzler, V.3    Hanauske-Abel, H.M.4    Kivirikko, K.I.5
  • 105
    • 0027666352 scopus 로고
    • Temporal and spatial regulation of 1-aminocyclopropane-1-carboxylate oxidase in the pollination-induced senescence of orchid flowers
    • Nadeau JA, Zhang XS, Nair H, O'Neill SD. 1993. Temporal and spatial regulation of 1-aminocyclopropane-1-carboxylate oxidase in the pollination-induced senescence of orchid flowers. Plant Physiol. 103: 31-39
    • (1993) Plant Physiol. , vol.103 , pp. 31-39
    • Nadeau, J.A.1    Zhang, X.S.2    Nair, H.3    O'Neill, S.D.4
  • 106
    • 0025949524 scopus 로고
    • Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2
    • Nagahama K, Ogawa T, Fujii T, Tazaki M, Tanase S, et al. 1991. Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2. J. Gen. Microb. 137:2281-86
    • (1991) J. Gen. Microb. , vol.137 , pp. 2281-2286
    • Nagahama, K.1    Ogawa, T.2    Fujii, T.3    Tazaki, M.4    Tanase, S.5
  • 109
    • 0028990109 scopus 로고
    • Photolysis of "purple" lipoxygenase: Implications for the structure of the chromophore
    • Nelson MJ, Chase DB, Seitz SP, 1995. Photolysis of "purple" lipoxygenase: implications for the structure of the chromophore. Biochemistry 34:6159-63
    • (1995) Biochemistry , vol.34 , pp. 6159-6163
    • Nelson, M.J.1    Chase, D.B.2    Seitz, S.P.3
  • 111
    • 0025081985 scopus 로고
    • Stereochemical nature of the products of linoleic acid oxidation catalyzed by lipoxygenases from potato and soybean
    • Nikolaev V, Reddanna P, Whelan J, Hildenbrandt G, Reddy CC. 1990. Stereochemical nature of the products of linoleic acid oxidation catalyzed by lipoxygenases from potato and soybean. Biochem. Biophys. Res. Commun. 170:491-96
    • (1990) Biochem. Biophys. Res. Commun. , vol.170 , pp. 491-496
    • Nikolaev, V.1    Reddanna, P.2    Whelan, J.3    Hildenbrandt, G.4    Reddy, C.C.5
  • 112
    • 0028468470 scopus 로고
    • Adioxygenase gene (Ids2) expressed under iron deficiency conditions in the roots of Hordeum vulgare
    • Okumura N, Nishizawa N-K, Umehara Y, Ohata T, Nakanishi H, et al. 1994. Adioxygenase gene (Ids2) expressed under iron deficiency conditions in the roots of Hordeum vulgare. Plant Mol. Biol. 25:705-19
    • (1994) Plant Mol. Biol. , vol.25 , pp. 705-719
    • Okumura, N.1    Nishizawa, N.-K.2    Umehara, Y.3    Ohata, T.4    Nakanishi, H.5
  • 113
    • 0001571157 scopus 로고
    • The control of ethylene in plant growth and development
    • ed. H Clijsters, M De Proft, R Marcelle. M van Poucke, Dordrecht: Kluwer
    • Osborne DJ. 1989. The control of ethylene in plant growth and development. In Biochemical and Physiological Aspects of Ethylene Production in Lower and Higher Plants, ed. H Clijsters, M De Proft, R Marcelle. M van Poucke, pp. 1-11. Dordrecht: Kluwer
    • (1989) Biochemical and Physiological Aspects of Ethylene Production in Lower and Higher Plants , pp. 1-11
    • Osborne, D.J.1
  • 115
    • 0029294087 scopus 로고
    • Sequential induction of the ethylene biosynthetic enzymes by indole-3-acetic acid in etiolated peas
    • Peck SC, Kende H. 1995. Sequential induction of the ethylene biosynthetic enzymes by indole-3-acetic acid in etiolated peas. Plant Mol. Biol. 28:293-301
    • (1995) Plant Mol. Biol. , vol.28 , pp. 293-301
    • Peck, S.C.1    Kende, H.2
  • 116
    • 0003444993 scopus 로고
    • Localization of the ethylene-forming enzyme from tomatoes, 1-aminocyclopropane-1-carboxylate oxidase, in transgenic yeast
    • Peck SC, Reinhardt D, Olson DC, Boller T, Kende H. 1992. Localization of the ethylene-forming enzyme from tomatoes, 1-aminocyclopropane-1-carboxylate oxidase, in transgenic yeast. J. Plant Physiol. 140:681-86
    • (1992) J. Plant Physiol. , vol.140 , pp. 681-686
    • Peck, S.C.1    Reinhardt, D.2    Olson, D.C.3    Boller, T.4    Kende, H.5
  • 117
    • 0000763890 scopus 로고
    • An antisense gene stimulates ethylene hormone production during tomato fruit ripening
    • Peñarrubia L, Aguilar M, Margossian L, Fischer RL. 1992. An antisense gene stimulates ethylene hormone production during tomato fruit ripening. Plant Cell 4:681-87
    • (1992) Plant Cell , vol.4 , pp. 681-687
    • Peñarrubia, L.1    Aguilar, M.2    Margossian, L.3    Fischer, R.L.4
  • 119
    • 0029328573 scopus 로고
    • Isolation and expression of three gibberellin 20-oxidase cDNA clones from Arabidopsis
    • Phillips AL. Ward DA, Uknes S. Appleford NEJ, Lange T, et al. 1995. Isolation and expression of three gibberellin 20-oxidase cDNA clones from Arabidopsis. Plant Physiol. 108:1049-57
    • (1995) Plant Physiol. , vol.108 , pp. 1049-1057
    • Phillips, A.L.1    Ward, D.A.2    Uknes, S.3    Appleford, N.E.J.4    Lange, T.5
  • 120
    • 0027185877 scopus 로고
    • Purification and properties of theapple fruit ethylene-forming enzyme
    • Pirrung MC, Kaiser LM, Chen J. 1993. Purification and properties of theapple fruit ethylene-forming enzyme. Biochemistry 32:7445-50
    • (1993) Biochemistry , vol.32 , pp. 7445-7450
    • Pirrung, M.C.1    Kaiser, L.M.2    Chen, J.3
  • 121
    • 0029310527 scopus 로고
    • Differential expression of two 1-aminocyclopropane-1-caiboxylic acid oxidase genes in broccoli after harvest
    • Pogson BJ, Downs CG, Davies KM. 1995. Differential expression of two 1-aminocyclopropane-1-caiboxylic acid oxidase genes in broccoli after harvest. Plant Physiol. 108:651-57
    • (1995) Plant Physiol. , vol.108 , pp. 651-657
    • Pogson, B.J.1    Downs, C.G.2    Davies, K.M.3
  • 122
    • 0027137336 scopus 로고
    • Carbon dioxide activation of 1-aminocyclopropane1-carboxylate (ACC) oxidase in ethylene synthesis
    • Poneleit LS, Dilley DR. 1993. Carbon dioxide activation of 1-aminocyclopropane1-carboxylate (ACC) oxidase in ethylene synthesis. Postharvest Biol. Technol. 3: 191-99
    • (1993) Postharvest Biol. Technol. , vol.3 , pp. 191-199
    • Poneleit, L.S.1    Dilley, D.R.2
  • 123
    • 0000658037 scopus 로고
    • A dilemma of dioxygenases (or where biochemistry and molecular biology fail to meet)
    • Prescott AG. 1993. A dilemma of dioxygenases (or where biochemistry and molecular biology fail to meet). J. Exp. Bot. 44:849-61
    • (1993) J. Exp. Bot. , vol.44 , pp. 849-861
    • Prescott, A.G.1
  • 124
    • 0009616002 scopus 로고
    • Inter-tissue complementation: A simple technique for direct analysis of gene-action sequence
    • Reddy GM, Coe EH Jr. 1962. Inter-tissue complementation: a simple technique for direct analysis of gene-action sequence. Science 138:149-50
    • (1962) Science , vol.138 , pp. 149-150
    • Reddy, G.M.1    Coe Jr., E.H.2
  • 125
    • 0028311824 scopus 로고
    • Subcellular localization of 1-aminocyclopropane-1-carboxylate oxidase in tomato cells
    • Reinhardt D, Kende H, Boller T. 1994. Subcellular localization of 1-aminocyclopropane-1-carboxylate oxidase in tomato cells. Planta 195:142-46
    • (1994) Planta , vol.195 , pp. 142-146
    • Reinhardt, D.1    Kende, H.2    Boller, T.3
  • 126
    • 0029038392 scopus 로고
    • Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes
    • Roach PL, Clifton IJ, Fülöp V, Harlos K, Barton GJ, et al. 1995. Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes. Nature 375:700-4
    • (1995) Nature , vol.375 , pp. 700-704
    • Roach, P.L.1    Clifton, I.J.2    Fülöp, V.3    Harlos, K.4    Barton, G.J.5
  • 128
    • 0028112281 scopus 로고
    • Immunocytolocalization of 1-aminocyclopropane-1-carboxylic acid oxidase in tomato and apple fruit
    • Rombaldi C, Lelièvre J-M, Latché A, Petitprez M, Bouzayen M, Pech J-C. 1994. Immunocytolocalization of 1-aminocyclopropane-1-carboxylic acid oxidase in tomato and apple fruit. Planta 192:453-60
    • (1994) Planta , vol.192 , pp. 453-460
    • Rombaldi, C.1    Lelièvre, J.-M.2    Latché, A.3    Petitprez, M.4    Bouzayen, M.5    Pech, J.-C.6
  • 129
    • 0028139568 scopus 로고
    • 2 levels reduce ethylene production in kiwifruit
    • 2 levels reduce ethylene production in kiwifruit. Physiol. Plant. 92:1-8
    • (1994) Physiol. Plant , vol.92 , pp. 1-8
    • Rothan, C.1    Nichols, J.2
  • 130
    • 0028039145 scopus 로고
    • The action of ascorbate in vesicular systems
    • Rubinstein B. 1994. The action of ascorbate in vesicular systems. J. Bioenerg. Biomembr. 26:385-91
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 385-391
    • Rubinstein, B.1
  • 132
    • 0028639234 scopus 로고
    • X-ray spectroscopy of the iron site in soybean lipoxygenase-1: Changes in coordination upon oxidation or addition of methanol
    • Scarrow RC, Trimitsis MG, Buck CP, Grove GN, Cowling RA, Nelson MJ. 1994. X-ray spectroscopy of the iron site in soybean lipoxygenase-1: changes in coordination upon oxidation or addition of methanol. Biochemistry 33:15023-35
    • (1994) Biochemistry , vol.33 , pp. 15023-15035
    • Scarrow, R.C.1    Trimitsis, M.G.2    Buck, C.P.3    Grove, G.N.4    Cowling, R.A.5    Nelson, M.J.6
  • 133
    • 0028209428 scopus 로고
    • The dioxygenation rate in lipoxygenase catalysis is determined by the amount of iron (III) lipoxygenase in solution
    • Schilstra MJ, Veldink GA, Vliegenthart JFG. 1994. The dioxygenation rate in lipoxygenase catalysis is determined by the amount of iron (III) lipoxygenase in solution. Biochemistry 33:3974-79
    • (1994) Biochemistry , vol.33 , pp. 3974-3979
    • Schilstra, M.J.1    Veldink, G.A.2    Vliegenthart, J.F.G.3
  • 134
    • 0027452908 scopus 로고
    • SC-0051, a 2-benzoyl-cyclohexane-1,3-dione bleaching herbicide is a potent inhibitor of the enzyme p-hydroxyphenylpyruvate dioxygenase
    • Schulz A, Ort O, Beyer P, Kleinig H. 1993. SC-0051, a 2-benzoyl-cyclohexane-1,3-dione bleaching herbicide is a potent inhibitor of the enzyme p-hydroxyphenylpyruvate dioxygenase. FEBS Lett. 318:162-66
    • (1993) FEBS Lett. , vol.318 , pp. 162-166
    • Schulz, A.1    Ort, O.2    Beyer, P.3    Kleinig, H.4
  • 135
    • 0028313670 scopus 로고
    • Inhibition of barnyardgrass 4-hydroxyphenylpyruvate dioxygenase by sulcotrione
    • Secor J. 1994. Inhibition of barnyardgrass 4-hydroxyphenylpyruvate dioxygenase by sulcotrione. Plant Physiol. 106:1429-33
    • (1994) Plant Physiol. , vol.106 , pp. 1429-1433
    • Secor, J.1
  • 136
    • 0026110717 scopus 로고
    • Nucleotide sequences of a soybean lipoxygenase gene and the short intergenic region between an upstream lipoxygenase gene
    • Shibata D, Kato T, Tanaka K. 1991. Nucleotide sequences of a soybean lipoxygenase gene and the short intergenic region between an upstream lipoxygenase gene. Plant Mol. Biol. 16:353-59
    • (1991) Plant Mol. Biol. , vol.16 , pp. 353-359
    • Shibata, D.1    Kato, T.2    Tanaka, K.3
  • 137
    • 0010008102 scopus 로고
    • Enzyme with dual lipoxygenase activities catalyzes leukotriene A4 synthesis from arachidonic acid
    • Shimizu T, Rådmark O, Samuelsson B. 1984. Enzyme with dual lipoxygenase activities catalyzes leukotriene A4 synthesis from arachidonic acid. Proc. Natl. Acad. Sci. USA 81:689-93
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 689-693
    • Shimizu, T.1    Rådmark, O.2    Samuelsson, B.3
  • 138
    • 0025840492 scopus 로고
    • Molecular J cloning of a putative plant endomembrane protein resembling vertebrate protein disulphide-isomerase and a phosphatidylinositol-specific phospholipase C
    • Shorrosh BS, Dixon RA. 1991. Molecular J cloning of a putative plant endomembrane protein resembling vertebrate protein disulphide-isomerase and a phosphatidylinositol-specific phospholipase C. Proc. Natl. Acad. Sci. USA 88:10941-45
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10941-10945
    • Shorrosh, B.S.1    Dixon, R.A.2
  • 140
    • 0000050279 scopus 로고
    • Activation of 1-aminocyclopropane-1-carboxylate oxidase by bicarbonate/carbon dioxide
    • Smith JJ, John P. 1993. Activation of 1-aminocyclopropane-1-carboxylate oxidase by bicarbonate/carbon dioxide. Phytochemistry 32:1381-86
    • (1993) Phytochemistry , vol.32 , pp. 1381-1386
    • Smith, J.J.1    John, P.2
  • 142
    • 0000548537 scopus 로고
    • Characterization of the ethylene-forming enzyme partially purified from melon
    • Smith JJ, Ververidis P, John P. 1992. Characterization of the ethylene-forming enzyme partially purified from melon. Phytochemistry 31:1485-94
    • (1992) Phytochemistry , vol.31 , pp. 1485-1494
    • Smith, J.J.1    Ververidis, P.2    John, P.3
  • 144
    • 0001900783 scopus 로고
    • 5
    • ed. N Takahashi, BO Phinney, J MacMillan, New York: Springer-Verlag
    • 5. In Gibberellins, ed. N Takahashi, BO Phinney, J MacMillan, pp. 62-71. New York: Springer-Verlag
    • (1990) Gibberellins , pp. 62-71
    • Smith, V.A.1    Albone, K.S.2    MacMillan, J.3
  • 146
    • 0040981833 scopus 로고
    • The partial purification and characterisation of gibberellin 2β-hydroxylases from seeds of Pisum sativum
    • Smith VA, MacMillan J. 1986. The partial purification and characterisation of gibberellin 2β-hydroxylases from seeds of Pisum sativum. Planta 167:9-18
    • (1986) Planta , vol.167 , pp. 9-18
    • Smith, V.A.1    MacMillan, J.2
  • 147
    • 0027323306 scopus 로고
    • Molecular cloning of an allene oxide synthase: A cytochrome P450 specialized for the metabolism of fatty acid hydroperoxides
    • Song W-C, Funk CD, Brash AR. 1993. Molecular cloning of an allene oxide synthase: a cytochrome P450 specialized for the metabolism of fatty acid hydroperoxides. Proc. Natl. Acad. Sci. USA 90: 8519-23
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8519-8523
    • Song, W.-C.1    Funk, C.D.2    Brash, A.R.3
  • 148
    • 0025873529 scopus 로고
    • Analysis and cloning of the ethylene-forming enzyme from tomato by functional expression of its mRNA in Xenopus laevis oocytes
    • Spanu P, Reinhardt D, Boiler T. 1991. Analysis and cloning of the ethylene-forming enzyme from tomato by functional expression of its mRNA in Xenopus laevis oocytes. EMBO J. 10:2007-13
    • (1991) EMBO J. , vol.10 , pp. 2007-2013
    • Spanu, P.1    Reinhardt, D.2    Boiler, T.3
  • 149
    • 0028386531 scopus 로고
    • Cloning and molecular analysis of structural genes involved in flavonoid and stilbene biosynthesis in grape (Vitis vinifera L. )
    • Sparvoli F, Martin C, Scienza A, Gavazzi G, Tonelli C. 1994. Cloning and molecular analysis of structural genes involved in flavonoid and stilbene biosynthesis in grape (Vitis vinifera L. ). Plant Mol. Biol. 24: 743-55
    • (1994) Plant Mol. Biol. , vol.24 , pp. 743-755
    • Sparvoli, F.1    Martin, C.2    Scienza, A.3    Gavazzi, G.4    Tonelli, C.5
  • 150
    • 0025911829 scopus 로고
    • Metalcatalyzed oxidation of proteins
    • Stadtman ER, Oliver CN. 1991. Metalcatalyzed oxidation of proteins. J. Biol. Chem. 266:2005-8
    • (1991) J. Biol. Chem. , vol.266 , pp. 2005-2008
    • Stadtman, E.R.1    Oliver, C.N.2
  • 151
    • 0001477970 scopus 로고
    • Flavonoid evolution: An enzymic approach
    • Stafford HA. 1991. Flavonoid evolution: an enzymic approach. Plant Physiol. 96: 680-85
    • (1991) Plant Physiol. , vol.96 , pp. 680-685
    • Stafford, H.A.1
  • 152
    • 0000333932 scopus 로고
    • Oxidation of flavanones to flavones with flower extracts of Antirrhinum majus (snapdragon)
    • Stotz G, Forkmann G. 1981. Oxidation of flavanones to flavones with flower extracts of Antirrhinum majus (snapdragon). Z. Naturforsch. 36c:737-41
    • (1981) Z. Naturforsch. , vol.36 C , pp. 737-741
    • Stotz, G.1    Forkmann, G.2
  • 154
    • 0025133298 scopus 로고
    • Endogenous gibberellins in Arabidopsis thaliana and possible steps blocked in the biosynthetic pathways of the semidwarf ga4 and ga5 mutants
    • Talon M, Koornneef M, Zeevaart JAD. 1990. Endogenous gibberellins in Arabidopsis thaliana and possible steps blocked in the biosynthetic pathways of the semidwarf ga4 and ga5 mutants. Proc. Natl. Acad. Sci. USA 87:7983-87
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7983-7987
    • Talon, M.1    Koornneef, M.2    Zeevaart, J.A.D.3
  • 155
    • 0027728944 scopus 로고
    • Organization and structure of the 1-aminocyclopropane-1-carboxylate oxidase gene family from Petunia hybrida
    • Tang X, Wang H, Brandt AS, Woodson WR. 1993. Organization and structure of the 1-aminocyclopropane-1-carboxylate oxidase gene family from Petunia hybrida. Plant Mol. Biol. 23:1151-64
    • (1993) Plant Mol. Biol. , vol.23 , pp. 1151-1164
    • Tang, X.1    Wang, H.2    Brandt, A.S.3    Woodson, W.R.4
  • 156
    • 0027725120 scopus 로고
    • A non-heme iron protein with heme tendencies: An investigation of the substrate specificity of thymine hydroxylase
    • Thornburg LD, Lai M-T, Wishnok JS, Stubbe J. 1993. A non-heme iron protein with heme tendencies: an investigation of the substrate specificity of thymine hydroxylase. Biochemistry 32:14023-33
    • (1993) Biochemistry , vol.32 , pp. 14023-14033
    • Thornburg, L.D.1    Lai, M.-T.2    Wishnok, J.S.3    Stubbe, J.4
  • 157
    • 33749103972 scopus 로고
    • Ascorbic acid in aromatic hydroxylation I: A model system for aromatic hydroxylation
    • Udenfriend S, Clark CT, Axelrod J, Brodie BB. 1954. Ascorbic acid in aromatic hydroxylation I: a model system for aromatic hydroxylation. J. Biol Chem. 208:731-39
    • (1954) J. Biol Chem. , vol.208 , pp. 731-739
    • Udenfriend, S.1    Clark, C.T.2    Axelrod, J.3    Brodie, B.B.4
  • 158
    • 0029013903 scopus 로고
    • Changes in the iron coordination sphere of Fe(II) lipoxygenase-1 from soybeans upon binding of linoleate or oleate
    • van der Heijdt LM, Schilstra MJ, Feiters MC, Nulting H-F, Hermes C, et al. 1995. Changes in the iron coordination sphere of Fe(II) lipoxygenase-1 from soybeans upon binding of linoleate or oleate. Eur. J. Biochem. 231:186-91
    • (1995) Eur. J. Biochem. , vol.231 , pp. 186-191
    • Van Der Heijdt, L.M.1    Schilstra, M.J.2    Feiters, M.C.3    Nulting, H.-F.4    Hermes, C.5
  • 159
    • 0000174065 scopus 로고
    • Complete recovery in vitro of ethylene-forming enzyme activity
    • Ververidis P, John P. 1991. Complete recovery in vitro of ethylene-forming enzyme activity. Phytochemistry 30:725-27
    • (1991) Phytochemistry , vol.30 , pp. 725-727
    • Ververidis, P.1    John, P.2
  • 160
    • 0028038836 scopus 로고
    • Extraction and biochemical characterization of 1-aminocyclopropane-1-carboxylic acid oxidase from pear
    • Vioque B, Castellano JM. 1994. Extraction and biochemical characterization of 1-aminocyclopropane-1-carboxylic acid oxidase from pear. Physiol. Plant. 90:334-38
    • (1994) Physiol. Plant , vol.90 , pp. 334-338
    • Vioque, B.1    Castellano, J.M.2
  • 161
    • 0027652168 scopus 로고
    • The petunia homologue of the Antirrhinum majus candi and Zea mays A2 flavonoid genes; homology to flavanone 3-hydroxylase and ethyleneforming enzyme
    • Weiss D, van der Luit AH, Kroon JTM, Mol JNM, Kooter JM. 1993. The petunia homologue of the Antirrhinum majus candi and Zea mays A2 flavonoid genes; homology to flavanone 3-hydroxylase and ethyleneforming enzyme. Plant Mol. Biol. 22: 893-97
    • (1993) Plant Mol. Biol. , vol.22 , pp. 893-897
    • Weiss, D.1    Van Der Luit, A.H.2    Kroon, J.T.M.3    Mol, J.N.M.4    Kooter, J.M.5
  • 162
    • 0027622793 scopus 로고
    • Apple ripening-related cDNA clone pAP4 confers ethylene-forming ability in transformed Saccharomyces cerevisiae
    • Wilson ID, Zhu Y, Burmeister DM, Dilley DR. 1993. Apple ripening-related cDNA clone pAP4 confers ethylene-forming ability in transformed Saccharomyces cerevisiae. Plant Physiol. 102:783-88
    • (1993) Plant Physiol. , vol.102 , pp. 783-788
    • Wilson, I.D.1    Zhu, Y.2    Burmeister, D.M.3    Dilley, D.R.4
  • 163
    • 0000601663 scopus 로고
    • Expression of ethylene biosynthetic pathway transcripts in senescing carnation flowers
    • Woodson WR, Park KY, Drory A, Larsen PB, Wang H. 1992. Expression of ethylene biosynthetic pathway transcripts in senescing carnation flowers. Plant Physiol. 99: 526-32
    • (1992) Plant Physiol. , vol.99 , pp. 526-532
    • Woodson, W.R.1    Park, K.Y.2    Drory, A.3    Larsen, P.B.4    Wang, H.5
  • 164
    • 0029046366 scopus 로고
    • The GA5 locus of Arabidopsis thaliana encodes a mullifunctional gibberellin 20-oxidase: Molecular cloning and functional expression
    • Xu Y-L, Li L, Wu K, Peeters AJM, Gage DA, Zeevaart JAD. 1995. The GA5 locus of Arabidopsis thaliana encodes a mullifunctional gibberellin 20-oxidase: molecular cloning and functional expression. Proc. Natl. Acad. Sci. USA 92:6640-44
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6640-6644
    • Xu, Y.-L.1    Li, L.2    Wu, K.3    Peeters, A.J.M.4    Gage, D.A.5    Zeevaart, J.A.D.6
  • 165
    • 0026480564 scopus 로고
    • Mammalian lipoxygenases: Molecular structures and functions
    • Yamamoto S. 1992. Mammalian lipoxygenases: molecular structures and functions. Biochim. Biophys. Acta 1128:117-31
    • (1992) Biochim. Biophys. Acta , vol.1128 , pp. 117-131
    • Yamamoto, S.1
  • 166
    • 0001642094 scopus 로고
    • Endogenous gibberellins from sporophyles of two tree ferns, Cibotium glaucum and Dicksonia antarctica
    • Yamane H, Fujioka S, Spray CR. Phinney BO, MacMillan J, el al. 1988. Endogenous gibberellins from sporophyles of two tree ferns, Cibotium glaucum and Dicksonia antarctica. Plant Physiol. 86:857-62
    • (1988) Plant Physiol. , vol.86 , pp. 857-862
    • Yamane, H.1    Fujioka, S.2    Spray, C.R.3    Phinney, B.O.4    MacMillan, J.5
  • 167
    • 0000750182 scopus 로고
    • Isolation and characterization of a soybean (Glycine max) lipoxygenase-3 gene
    • Yenofsky RL, Fine M, Liu C. 1988. Isolation and characterization of a soybean (Glycine max) lipoxygenase-3 gene. Mol. Gen. Genet. 211:215-22
    • (1988) Mol. Gen. Genet. , vol.211 , pp. 215-222
    • Yenofsky, R.L.1    Fine, M.2    Liu, C.3
  • 168
    • 0027078552 scopus 로고
    • Melabolic engineering of medicinal plants: Transgenic Atropa belladonna with an improved alkaloid composition
    • Yun D-J, Hashimoto T, Yamada Y. 1992. Melabolic engineering of medicinal plants: transgenic Atropa belladonna with an improved alkaloid composition. Proc. Natl. Acad. Sci. USA 89:11799-803
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11799-11803
    • Yun, D.-J.1    Hashimoto, T.2    Yamada, Y.3
  • 169
    • 0028946280 scopus 로고
    • Expression, purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from tomato in Escherichia coli
    • Zhang Z, Schofield CJ, Baldwin JE, Thomas P, John P. 1995. Expression, purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from tomato in Escherichia coli. Biochem. J. 307: 77-85
    • (1995) Biochem. J. , vol.307 , pp. 77-85
    • Zhang, Z.1    Schofield, C.J.2    Baldwin, J.E.3    Thomas, P.4    John, P.5


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