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Volumn 70, Issue 13-14, 2009, Pages 1532-1538

Enzymes in jasmonate biosynthesis - Structure, function, regulation

Author keywords

Allene oxide cyclase; Allene oxide synthase; Crystal structure; CYP74; Jasmonate biosynthesis; Oxophytodienoate reductase; Oxylipins; Substrate specificity

Indexed keywords

CYCLOPENTANE DERIVATIVE; HYDROPEROXIDE ISOMERASE; ISOMERASE; JASMONIC ACID; OXYLIPIN; VEGETABLE PROTEIN;

EID: 70350507480     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2009.07.032     Document Type: Review
Times cited : (333)

References (82)
  • 1
    • 0032917707 scopus 로고    scopus 로고
    • Structure-activity analyses reveal the existence of two separate groups of active octadecanoids in elicitation of the tendril-coiling response of Bryonia dioica Jacq
    • Blechert S., Bockelmann C., Füßlein M., Von Schrader T., Stelmach B., Niesel U., and Weiler E.W. Structure-activity analyses reveal the existence of two separate groups of active octadecanoids in elicitation of the tendril-coiling response of Bryonia dioica Jacq. Planta 207 (1999) 470-479
    • (1999) Planta , vol.207 , pp. 470-479
    • Blechert, S.1    Bockelmann, C.2    Füßlein, M.3    Von Schrader, T.4    Stelmach, B.5    Niesel, U.6    Weiler, E.W.7
  • 2
    • 0036633804 scopus 로고    scopus 로고
    • Impact of phyto-oxylipins in plant defense
    • Blee E. Impact of phyto-oxylipins in plant defense. Trends Plant Sci. 7 (2002) 315-321
    • (2002) Trends Plant Sci. , vol.7 , pp. 315-321
    • Blee, E.1
  • 3
    • 0001679525 scopus 로고
    • Isolation and characterization of natural allene oxides: unstable intermediates in the metabolism of lipid hydroperoxides
    • Brash A.R., Baertschi S.W., Ingram C.D., and Harris T.M. Isolation and characterization of natural allene oxides: unstable intermediates in the metabolism of lipid hydroperoxides. Proc. Natl. Acad. Sci. USA 85 (1988) 3382-3386
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3382-3386
    • Brash, A.R.1    Baertschi, S.W.2    Ingram, C.D.3    Harris, T.M.4
  • 4
    • 0034980393 scopus 로고    scopus 로고
    • X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE
    • Breithaupt C., Strassner J., Breitinger U., Huber R., Macheroux P., Schaller A., and Clausen T. X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE. Structure 9 (2001) 419-429
    • (2001) Structure , vol.9 , pp. 419-429
    • Breithaupt, C.1    Strassner, J.2    Breitinger, U.3    Huber, R.4    Macheroux, P.5    Schaller, A.6    Clausen, T.7
  • 7
    • 33645908170 scopus 로고    scopus 로고
    • Jasmonate: an oxylipin signal with many roles in plants
    • Browse J. Jasmonate: an oxylipin signal with many roles in plants. Vitam. Horm. 72 (2005) 431-456
    • (2005) Vitam. Horm. , vol.72 , pp. 431-456
    • Browse, J.1
  • 10
    • 48949107755 scopus 로고    scopus 로고
    • Regulation and function of Arabidopsis JASMONATE ZIM-Domain genes in response to wounding and herbivory
    • Chung H.S., Koo A.J.K., Gao X., Jayanty S., Thines B., Jones A.D., and Howe G.A. Regulation and function of Arabidopsis JASMONATE ZIM-Domain genes in response to wounding and herbivory. Plant Physiol. 146 (2008) 952-964
    • (2008) Plant Physiol. , vol.146 , pp. 952-964
    • Chung, H.S.1    Koo, A.J.K.2    Gao, X.3    Jayanty, S.4    Thines, B.5    Jones, A.D.6    Howe, G.A.7
  • 11
    • 2442648069 scopus 로고    scopus 로고
    • Gene-specific involvement of beta-oxidation in wound-activated responses in Arabidopsis
    • Cruz Castillo M., Martinez C., Buchala A., Metraux J.P., and Leon J. Gene-specific involvement of beta-oxidation in wound-activated responses in Arabidopsis. Plant Physiol. 135 (2004) 85-94
    • (2004) Plant Physiol. , vol.135 , pp. 85-94
    • Cruz Castillo, M.1    Martinez, C.2    Buchala, A.3    Metraux, J.P.4    Leon, J.5
  • 12
    • 23444445169 scopus 로고    scopus 로고
    • Dirigent phenoxy radical coupling: advances and challenges
    • Davin L.B., and Lewis N.G. Dirigent phenoxy radical coupling: advances and challenges. Curr. Opin. Biotech. 16 (2005) 398-406
    • (2005) Curr. Opin. Biotech. , vol.16 , pp. 398-406
    • Davin, L.B.1    Lewis, N.G.2
  • 13
    • 0031031957 scopus 로고    scopus 로고
    • Stereoselective bimolecular phenoxy radical coupling by an auxiliary (dirigent) protein without an active center
    • Davin L.B., Wang H.B., Crowell A.L., Bedgar D.L., Martin D.M., Sarkanen S., and Lewis N.G. Stereoselective bimolecular phenoxy radical coupling by an auxiliary (dirigent) protein without an active center. Science 275 (1997) 362-366
    • (1997) Science , vol.275 , pp. 362-366
    • Davin, L.B.1    Wang, H.B.2    Crowell, A.L.3    Bedgar, D.L.4    Martin, D.M.5    Sarkanen, S.6    Lewis, N.G.7
  • 15
    • 34249979246 scopus 로고    scopus 로고
    • Jasmonate biosynthesis in Arabidopsis thaliana requires peroxisomal beta-oxidation enzymes - additional proof by properties of pex6 and aim1
    • Delker C., Zolman B.K., Miersch O., and Wasternack C. Jasmonate biosynthesis in Arabidopsis thaliana requires peroxisomal beta-oxidation enzymes - additional proof by properties of pex6 and aim1. Phytochemistry 68 (2007) 1642-1650
    • (2007) Phytochemistry , vol.68 , pp. 1642-1650
    • Delker, C.1    Zolman, B.K.2    Miersch, O.3    Wasternack, C.4
  • 16
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C.M. Protein folding and misfolding. Nature 426 (2003) 884-890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 19
    • 0034684168 scopus 로고    scopus 로고
    • The lipocalin protein family: structural and sequence overview
    • Flower D.R., North A.C., and Sansom C.E. The lipocalin protein family: structural and sequence overview. Biochim. Biophys. Acta 1482 (2000) 9-24
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 9-24
    • Flower, D.R.1    North, A.C.2    Sansom, C.E.3
  • 22
    • 0035144016 scopus 로고    scopus 로고
    • Tomato allene oxide synthase and fatty acid hydroperoxide lyase, two cytochrome P450s involved in oxylipin metabolism, are targeted to different membranes of chloroplast envelope
    • Froehlich J.E., Itoh A., and Howe G.A. Tomato allene oxide synthase and fatty acid hydroperoxide lyase, two cytochrome P450s involved in oxylipin metabolism, are targeted to different membranes of chloroplast envelope. Plant Physiol. 125 (2001) 306-317
    • (2001) Plant Physiol. , vol.125 , pp. 306-317
    • Froehlich, J.E.1    Itoh, A.2    Howe, G.A.3
  • 23
    • 47749121066 scopus 로고    scopus 로고
    • Spatial and temporal dynamics of jasmonate synthesis and accumulation in Arabidopsis in response to wounding
    • Glauser G., Grata E., Dubugnon L., Rudaz S., Farmer E.E., and Wolfender J.L. Spatial and temporal dynamics of jasmonate synthesis and accumulation in Arabidopsis in response to wounding. J. Biol. Chem. 283 (2008) 16400-16407
    • (2008) J. Biol. Chem. , vol.283 , pp. 16400-16407
    • Glauser, G.1    Grata, E.2    Dubugnon, L.3    Rudaz, S.4    Farmer, E.E.5    Wolfender, J.L.6
  • 24
    • 0025159426 scopus 로고
    • Allene oxide cyclase: a new enzyme in plant lipid metabolism
    • Hamberg M., and Fahlstadius P. Allene oxide cyclase: a new enzyme in plant lipid metabolism. Arch. Biochem. Biophys. 276 (1990) 518-526
    • (1990) Arch. Biochem. Biophys. , vol.276 , pp. 518-526
    • Hamberg, M.1    Fahlstadius, P.2
  • 25
    • 0142121372 scopus 로고    scopus 로고
    • Occurrence of the allene oxide cyclase in different organs and tissues of Arabidopsis thaliana
    • Hause B., Stenzel I., Miersch O., and Wasternack C. Occurrence of the allene oxide cyclase in different organs and tissues of Arabidopsis thaliana. Phytochemistry 64 (2003) 971-980
    • (2003) Phytochemistry , vol.64 , pp. 971-980
    • Hause, B.1    Stenzel, I.2    Miersch, O.3    Wasternack, C.4
  • 27
    • 40849111441 scopus 로고    scopus 로고
    • Molecular mechanism of enzymatic allene oxide cyclization in plants
    • Hofmann E., and Pollmann S. Molecular mechanism of enzymatic allene oxide cyclization in plants. Plant Physiol. Biochem. 46 (2008) 302-308
    • (2008) Plant Physiol. Biochem. , vol.46 , pp. 302-308
    • Hofmann, E.1    Pollmann, S.2
  • 28
    • 33845801592 scopus 로고    scopus 로고
    • The crystal structure of Arabidopsis thaliana allene oxide cyclase: insights into the oxylipin cyclization reaction
    • Hofmann E., Zerbe P., and Schaller F. The crystal structure of Arabidopsis thaliana allene oxide cyclase: insights into the oxylipin cyclization reaction. Plant Cell 18 (2006) 3201-3217
    • (2006) Plant Cell , vol.18 , pp. 3201-3217
    • Hofmann, E.1    Zerbe, P.2    Schaller, F.3
  • 30
    • 0343193114 scopus 로고    scopus 로고
    • Cytochrome P450-dependent metabolism of oxylipins in tomato. Cloning and expression of allene oxide synthase and fatty acid hydroperoxide lyase
    • Howe G.A., Lee G.I., Itoh A., Li L., and DeRocher A.E. Cytochrome P450-dependent metabolism of oxylipins in tomato. Cloning and expression of allene oxide synthase and fatty acid hydroperoxide lyase. Plant Physiol. 123 (2000) 711-724
    • (2000) Plant Physiol. , vol.123 , pp. 711-724
    • Howe, G.A.1    Lee, G.I.2    Itoh, A.3    Li, L.4    DeRocher, A.E.5
  • 31
    • 33947424280 scopus 로고    scopus 로고
    • Transcript profile of transgenic Arabidopsis constitutively producing methyl jasmonate
    • Jung C., Yeu S.Y., Koo Y.J., Kim M., Do Choi Y., and Cheong J.J. Transcript profile of transgenic Arabidopsis constitutively producing methyl jasmonate. J. Plant Biol. 50 (2007) 12-17
    • (2007) J. Plant Biol. , vol.50 , pp. 12-17
    • Jung, C.1    Yeu, S.Y.2    Koo, Y.J.3    Kim, M.4    Do Choi, Y.5    Cheong, J.J.6
  • 32
    • 41649116914 scopus 로고    scopus 로고
    • Jasmonates meet fatty acids: functional analysis of a new acyl-coenzyme A synthetase family from Arabidopsis thaliana
    • Kienow L., Schneider K., Bartsch M., Stuible H.-P., Weng H., Miersch O., Wasternack C., and Kombrink E. Jasmonates meet fatty acids: functional analysis of a new acyl-coenzyme A synthetase family from Arabidopsis thaliana. J. Exp. Bot. 59 (2008) 403-419
    • (2008) J. Exp. Bot. , vol.59 , pp. 403-419
    • Kienow, L.1    Schneider, K.2    Bartsch, M.3    Stuible, H.-P.4    Weng, H.5    Miersch, O.6    Wasternack, C.7    Kombrink, E.8
  • 33
    • 33845678408 scopus 로고    scopus 로고
    • Identification of a peroxisomal acyl-activating enzyme involved in the biosynthesis of jasmonic acid in Arabidopsis
    • Koo A.J.K., Chung H.S., Kobayashi Y., and Howe G.A. Identification of a peroxisomal acyl-activating enzyme involved in the biosynthesis of jasmonic acid in Arabidopsis. J. Biol. Chem. 281 (2006) 33511-33520
    • (2006) J. Biol. Chem. , vol.281 , pp. 33511-33520
    • Koo, A.J.K.1    Chung, H.S.2    Kobayashi, Y.3    Howe, G.A.4
  • 34
    • 0030152391 scopus 로고    scopus 로고
    • Cloning, molecular and functional characterization of Arabidopsis thaliana allene oxide synthase (CYP74), the first enzyme of the octadecanoid pathway to jasmonates
    • Laudert D., Pfannschmidt U., Lottspeich F., Holländer-Czytko H., and Weiler E.W. Cloning, molecular and functional characterization of Arabidopsis thaliana allene oxide synthase (CYP74), the first enzyme of the octadecanoid pathway to jasmonates. Plant Mol. Biol. 31 (1996) 323-335
    • (1996) Plant Mol. Biol. , vol.31 , pp. 323-335
    • Laudert, D.1    Pfannschmidt, U.2    Lottspeich, F.3    Holländer-Czytko, H.4    Weiler, E.W.5
  • 35
    • 0031569411 scopus 로고    scopus 로고
    • Analysis of 12-oxo-phytodienoic acid enantiomers in biological samples by capillary gas chromatography-mass spectrometry using cyclodextrin stationary phases
    • Laudert D., Hennig P., Stelmach B.A., Müller A., Andert L., and Weiler E.W. Analysis of 12-oxo-phytodienoic acid enantiomers in biological samples by capillary gas chromatography-mass spectrometry using cyclodextrin stationary phases. Anal. Biochem. 246 (1997) 211-217
    • (1997) Anal. Biochem. , vol.246 , pp. 211-217
    • Laudert, D.1    Hennig, P.2    Stelmach, B.A.3    Müller, A.4    Andert, L.5    Weiler, E.W.6
  • 36
    • 0033921659 scopus 로고    scopus 로고
    • Transgenic Nicotiana tabacum and Arabidopsis thaliana plants overexpressing allene oxide synthase
    • Laudert D., Schaller F., and Weiler E.W. Transgenic Nicotiana tabacum and Arabidopsis thaliana plants overexpressing allene oxide synthase. Planta 211 (2000) 163-165
    • (2000) Planta , vol.211 , pp. 163-165
    • Laudert, D.1    Schaller, F.2    Weiler, E.W.3
  • 37
    • 52149110322 scopus 로고    scopus 로고
    • Structural insights into the evolutionary paths of oxylipin biosynthetic enzymes
    • Lee D.S., Nioche P., Hamberg M., and Raman C.S. Structural insights into the evolutionary paths of oxylipin biosynthetic enzymes. Nature 455 (2008) 363-368
    • (2008) Nature , vol.455 , pp. 363-368
    • Lee, D.S.1    Nioche, P.2    Hamberg, M.3    Raman, C.S.4
  • 38
    • 34548387498 scopus 로고    scopus 로고
    • Ensemble refinement of protein crystal structures: validation and application
    • Levin E.J., Kondrashov D.A., Wesenberg G.E., and Phillips G.N. Ensemble refinement of protein crystal structures: validation and application. Structure 15 (2007) 1040-1052
    • (2007) Structure , vol.15 , pp. 1040-1052
    • Levin, E.J.1    Kondrashov, D.A.2    Wesenberg, G.E.3    Phillips, G.N.4
  • 39
    • 0842291761 scopus 로고    scopus 로고
    • The tomato homolog of CORONATINE-INSENSITIVE1 is required for the maternal control of seed maturation, jasmonate-signaled defense responses, and glandular trichome development
    • Li L., Zhao Y., McCaig B.C., Wingerd B.A., Wang J., Whalon M.E., Pichersky E., and Howe G.A. The tomato homolog of CORONATINE-INSENSITIVE1 is required for the maternal control of seed maturation, jasmonate-signaled defense responses, and glandular trichome development. Plant Cell 16 (2004) 126-143
    • (2004) Plant Cell , vol.16 , pp. 126-143
    • Li, L.1    Zhao, Y.2    McCaig, B.C.3    Wingerd, B.A.4    Wang, J.5    Whalon, M.E.6    Pichersky, E.7    Howe, G.A.8
  • 41
    • 52949127334 scopus 로고    scopus 로고
    • Modes of heme binding and substrate access for cytochrome P450 CYP74A revealed by crystal structures of allene oxide synthase
    • Li L., Chang Z., Pan Z., Fu Z.Q., and Wang X. Modes of heme binding and substrate access for cytochrome P450 CYP74A revealed by crystal structures of allene oxide synthase. Proc. Natl. Acad. Sci. USA 105 (2008) 13883-13888
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 13883-13888
    • Li, L.1    Chang, Z.2    Pan, Z.3    Fu, Z.Q.4    Wang, X.5
  • 43
    • 64749095818 scopus 로고    scopus 로고
    • Oxylipins: structurally diverse metabolites from fatty acid oxidation
    • Mosblech A., Feussner I., and Heilmann I. Oxylipins: structurally diverse metabolites from fatty acid oxidation. Plant Physiol. Biochem. 47 (2009) 511-517
    • (2009) Plant Physiol. Biochem. , vol.47 , pp. 511-517
    • Mosblech, A.1    Feussner, I.2    Heilmann, I.3
  • 44
    • 3042720445 scopus 로고    scopus 로고
    • Archetype signals in plants: the phytoprostanes
    • Mueller M.J. Archetype signals in plants: the phytoprostanes. Curr. Opin. Plant. Biol. 7 (2004) 441-448
    • (2004) Curr. Opin. Plant. Biol. , vol.7 , pp. 441-448
    • Mueller, M.J.1
  • 46
    • 0035984161 scopus 로고    scopus 로고
    • A knock-out mutation in allene oxide synthase results in male sterility and defective wound signal transduction in Arabidopsis due to a block in jasmonic acid biosynthesis
    • Park J.H., Halitschke R., Kim H.B., Baldwin I.T., Feldmann K.A., and Feyereisen R. A knock-out mutation in allene oxide synthase results in male sterility and defective wound signal transduction in Arabidopsis due to a block in jasmonic acid biosynthesis. Plant J. 31 (2002) 1-12
    • (2002) Plant J. , vol.31 , pp. 1-12
    • Park, J.H.1    Halitschke, R.2    Kim, H.B.3    Baldwin, I.T.4    Feldmann, K.A.5    Feyereisen, R.6
  • 47
    • 0343962242 scopus 로고    scopus 로고
    • The Arabidopsis DELAYED DEHISCENCE1 gene encodes an enzyme in the jasmonic acid synthesis pathway
    • Sanders P.M., Lee P.Y., Biesgen C., Boone J.D., Beals T.P., Weiler E.W., and Goldberg R.B. The Arabidopsis DELAYED DEHISCENCE1 gene encodes an enzyme in the jasmonic acid synthesis pathway. Plant Cell 12 (2000) 1042-1061
    • (2000) Plant Cell , vol.12 , pp. 1042-1061
    • Sanders, P.M.1    Lee, P.Y.2    Biesgen, C.3    Boone, J.D.4    Beals, T.P.5    Weiler, E.W.6    Goldberg, R.B.7
  • 48
    • 67649719540 scopus 로고    scopus 로고
    • Jasmonate biosynthesis and signaling for induced plant defense against herbivory
    • Schaller A. (Ed), Springer, Heidelberg
    • Schaller A., and Stintzi A. Jasmonate biosynthesis and signaling for induced plant defense against herbivory. In: Schaller A. (Ed). Induced Plant Resistance Against Herbivory (2008), Springer, Heidelberg 349-365
    • (2008) Induced Plant Resistance Against Herbivory , pp. 349-365
    • Schaller, A.1    Stintzi, A.2
  • 49
    • 0030869796 scopus 로고    scopus 로고
    • Molecular cloning and characterization of 12-oxophytodienoate reductase, an enzyme of the octadecanoid signaling pathway from Arabidopsis thaliana. Structural and functional relationship to yeast old yellow enzyme
    • Schaller F., and Weiler E.W. Molecular cloning and characterization of 12-oxophytodienoate reductase, an enzyme of the octadecanoid signaling pathway from Arabidopsis thaliana. Structural and functional relationship to yeast old yellow enzyme. J. Biol. Chem. 272 (1997) 28066-28072
    • (1997) J. Biol. Chem. , vol.272 , pp. 28066-28072
    • Schaller, F.1    Weiler, E.W.2
  • 50
    • 0034031727 scopus 로고    scopus 로고
    • 12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in jasmonate biosynthesis
    • Schaller F., Biesgen C., Müssig C., Altmann T., and Weiler E.W. 12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in jasmonate biosynthesis. Planta 210 (2000) 979-984
    • (2000) Planta , vol.210 , pp. 979-984
    • Schaller, F.1    Biesgen, C.2    Müssig, C.3    Altmann, T.4    Weiler, E.W.5
  • 52
    • 42649119765 scopus 로고    scopus 로고
    • The allene oxide cyclase family of Arabidopsis thaliana - localization and cyclization
    • Schaller F., Zerbe P., Reinbothe S., Reinbothe C., Hofmann E., and Pollmann S. The allene oxide cyclase family of Arabidopsis thaliana - localization and cyclization. FEBS J. 275 (2008) 2428-2441
    • (2008) FEBS J. , vol.275 , pp. 2428-2441
    • Schaller, F.1    Zerbe, P.2    Reinbothe, S.3    Reinbothe, C.4    Hofmann, E.5    Pollmann, S.6
  • 54
    • 34247185391 scopus 로고    scopus 로고
    • Functional diversification of acyl-coenzyme A oxidases in jasmonic acid biosynthesis and action
    • Schilmiller A.L., Koo A.J.K., and Howe G.A. Functional diversification of acyl-coenzyme A oxidases in jasmonic acid biosynthesis and action. Plant Physiol. 143 (2007) 812-824
    • (2007) Plant Physiol. , vol.143 , pp. 812-824
    • Schilmiller, A.L.1    Koo, A.J.K.2    Howe, G.A.3
  • 55
    • 17144416797 scopus 로고    scopus 로고
    • A new type of peroxisomal acyl-coenzyme A synthetase from Arabidopsis thaliana has the catalytic capacity to activate biosynthetic precursors of jasmonic acid
    • Schneider K., Kienow L., Schmelzer E., Colby T., Bartsch M., Miersch O., Wasternack C., Kombrink E., and Stuible H.P. A new type of peroxisomal acyl-coenzyme A synthetase from Arabidopsis thaliana has the catalytic capacity to activate biosynthetic precursors of jasmonic acid. J. Biol. Chem. 280 (2005) 13962-13972
    • (2005) J. Biol. Chem. , vol.280 , pp. 13962-13972
    • Schneider, K.1    Kienow, L.2    Schmelzer, E.3    Colby, T.4    Bartsch, M.5    Miersch, O.6    Wasternack, C.7    Kombrink, E.8    Stuible, H.P.9
  • 56
    • 0038796765 scopus 로고    scopus 로고
    • Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases
    • Shockey J.M., Fulda M.S., and Browse J. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 132 (2003) 1065-1076
    • (2003) Plant Physiol. , vol.132 , pp. 1065-1076
    • Shockey, J.M.1    Fulda, M.S.2    Browse, J.3
  • 57
    • 0033997249 scopus 로고    scopus 로고
    • Expression of allene oxide synthase determines defense gene activation in tomato
    • Sivasankar S., Sheldrick B., and Rothstein S.J. Expression of allene oxide synthase determines defense gene activation in tomato. Plant Physiol. 122 (2000) 1335-1342
    • (2000) Plant Physiol. , vol.122 , pp. 1335-1342
    • Sivasankar, S.1    Sheldrick, B.2    Rothstein, S.J.3
  • 59
    • 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 C.D., and Brash A.R. Molecular cloning of an allene oxide synthase: a cytochrome P450 specialized for the metabolism of fatty acid hydroperoxides. Proc. Natl. Acad. Sci. USA 90 (1993) 8519-8523
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8519-8523
    • Song, W.C.1    Funk, C.D.2    Brash, A.R.3
  • 60
    • 0037327731 scopus 로고    scopus 로고
    • Allene oxide cyclase dependence of the wound response and vascular bundle-specific generation of jasmonates in tomato - amplification in wound signalling
    • Stenzel I., Hause B., Maucher H., Pitzschke A., Miersch O., Ziegler J., Ryan C.A., and Wasternack C. Allene oxide cyclase dependence of the wound response and vascular bundle-specific generation of jasmonates in tomato - amplification in wound signalling. Plant J. 33 (2003) 577-589
    • (2003) Plant J. , vol.33 , pp. 577-589
    • Stenzel, I.1    Hause, B.2    Maucher, H.3    Pitzschke, A.4    Miersch, O.5    Ziegler, J.6    Ryan, C.A.7    Wasternack, C.8
  • 62
    • 0034641758 scopus 로고    scopus 로고
    • The Arabidopsis male-sterile mutant, opr3, lacks the 12-oxophytodienoic acid reductase required for jasmonate synthesis
    • Stintzi A., and Browse J. The Arabidopsis male-sterile mutant, opr3, lacks the 12-oxophytodienoic acid reductase required for jasmonate synthesis. Proc. Natl. Acad. Sci. USA 97 (2000) 10625-10630
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10625-10630
    • Stintzi, A.1    Browse, J.2
  • 64
    • 0041031592 scopus 로고    scopus 로고
    • A homolog of old yellow enzyme in tomato. Spectral properties and substrate specificity of the recombinant protein
    • Straßner J., Fürholz A., Macheroux P., Amrhein N., and Schaller A. A homolog of old yellow enzyme in tomato. Spectral properties and substrate specificity of the recombinant protein. J. Biol. Chem. 274 (1999) 35067-35073
    • (1999) J. Biol. Chem. , vol.274 , pp. 35067-35073
    • Straßner, J.1    Fürholz, A.2    Macheroux, P.3    Amrhein, N.4    Schaller, A.5
  • 65
    • 0010632418 scopus 로고    scopus 로고
    • Characterization and cDNA-microarray expression analysis of 12-oxophytodienoate reductases reveals differential roles for octadecanoid biosynthesis in the local versus the systemic wound response
    • Strassner J., Schaller F., Frick U.B., Howe G.A., Weiler E.W., Amrhein N.A., Macheroux P., and Schaller A. Characterization and cDNA-microarray expression analysis of 12-oxophytodienoate reductases reveals differential roles for octadecanoid biosynthesis in the local versus the systemic wound response. Plant J. 32 (2002) 585-601
    • (2002) Plant J. , vol.32 , pp. 585-601
    • Strassner, J.1    Schaller, F.2    Frick, U.B.3    Howe, G.A.4    Weiler, E.W.5    Amrhein, N.A.6    Macheroux, P.7    Schaller, A.8
  • 66
    • 33845422008 scopus 로고    scopus 로고
    • Formation of oxylipins by CYP74 enzymes
    • Stumpe M., and Feussner I. Formation of oxylipins by CYP74 enzymes. Phytochem. Rev. 5 (2006) 347-357
    • (2006) Phytochem. Rev. , vol.5 , pp. 347-357
    • Stumpe, M.1    Feussner, I.2
  • 68
    • 20444476835 scopus 로고    scopus 로고
    • Jasmonoic acid levels are reduced in COMATOSE ATP-binding cassette transporter mutants. Implications for transport of jasmonate precursors into peroxisomes
    • Theodoulou F.L., Job K., Slocombe S.P., Footitt S., Holdsworth M., Baker A., Larson T.R., and Graham I.A. Jasmonoic acid levels are reduced in COMATOSE ATP-binding cassette transporter mutants. Implications for transport of jasmonate precursors into peroxisomes. Plant Physiol. 137 (2005) 835-840
    • (2005) Plant Physiol. , vol.137 , pp. 835-840
    • Theodoulou, F.L.1    Job, K.2    Slocombe, S.P.3    Footitt, S.4    Holdsworth, M.5    Baker, A.6    Larson, T.R.7    Graham, I.A.8
  • 69
    • 0034473821 scopus 로고    scopus 로고
    • Two families of acyl-CoA thioesterases in Arabidopsis
    • Tilton G., Shockey J., and Browse J. Two families of acyl-CoA thioesterases in Arabidopsis. Biochem. Soc. Trans. 28 (2000) 946-947
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 946-947
    • Tilton, G.1    Shockey, J.2    Browse, J.3
  • 70
    • 1542350187 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of ACH2, an acyl-CoA thioesterase from Arabidopsis thaliana
    • Tilton G.B., Shockey J.M., and Browse J. Biochemical and molecular characterization of ACH2, an acyl-CoA thioesterase from Arabidopsis thaliana. J. Biol. Chem. 279 (2004) 7487-7494
    • (2004) J. Biol. Chem. , vol.279 , pp. 7487-7494
    • Tilton, G.B.1    Shockey, J.M.2    Browse, J.3
  • 71
    • 53049095791 scopus 로고    scopus 로고
    • Determinants governing the CYP74 catalysis: conversion of allene oxide synthase into hydroperoxide lyase by site-directed mutagenesis
    • Toporkova Y.Y., Gogolev Y.V., Mukhtarova L.S., and Grechkin A.N. Determinants governing the CYP74 catalysis: conversion of allene oxide synthase into hydroperoxide lyase by site-directed mutagenesis. FEBS Lett. 582 (2008) 3423-3428
    • (2008) FEBS Lett. , vol.582 , pp. 3423-3428
    • Toporkova, Y.Y.1    Gogolev, Y.V.2    Mukhtarova, L.S.3    Grechkin, A.N.4
  • 72
    • 0001699831 scopus 로고
    • Biosynthesis of jasmonic acid by several plant species
    • Vick B.A., and Zimmerman D.C. Biosynthesis of jasmonic acid by several plant species. Plant Physiol. 75 (1984) 458-461
    • (1984) Plant Physiol. , vol.75 , pp. 458-461
    • Vick, B.A.1    Zimmerman, D.C.2
  • 73
    • 33744963538 scopus 로고    scopus 로고
    • Tocopherol cyclase (VTE1) localization and vitamin E accumulation in chloroplast plastoglobule lipoprotein particles
    • Vidi P.A., Kanwischer M., Baginsky S., Austin J.R., Csucs G., Dormann P., Kessler F., and Brehelin C. Tocopherol cyclase (VTE1) localization and vitamin E accumulation in chloroplast plastoglobule lipoprotein particles. J. Biol. Chem. 281 (2006) 11225-11234
    • (2006) J. Biol. Chem. , vol.281 , pp. 11225-11234
    • Vidi, P.A.1    Kanwischer, M.2    Baginsky, S.3    Austin, J.R.4    Csucs, G.5    Dormann, P.6    Kessler, F.7    Brehelin, C.8
  • 74
    • 0033167173 scopus 로고    scopus 로고
    • Overexpression of a cytoplasm-localized allene oxide synthase promotes the wound-induced accumulation of jasmonic acid in transgenic tobacco
    • Wang C., Avdiushko S., and Hildebrand D.F. Overexpression of a cytoplasm-localized allene oxide synthase promotes the wound-induced accumulation of jasmonic acid in transgenic tobacco. Plant Mol. Biol. 40 (1999) 783-793
    • (1999) Plant Mol. Biol. , vol.40 , pp. 783-793
    • Wang, C.1    Avdiushko, S.2    Hildebrand, D.F.3
  • 75
    • 34848897179 scopus 로고    scopus 로고
    • Jasmonates: an update on biosynthesis, signal transduction and action in plant stress response, growth and development
    • Wasternack C. Jasmonates: an update on biosynthesis, signal transduction and action in plant stress response, growth and development. Ann. Bot. 100 (2007) 681-697
    • (2007) Ann. Bot. , vol.100 , pp. 681-697
    • Wasternack, C.1
  • 76
    • 0030985416 scopus 로고    scopus 로고
    • Dinor-oxo-phytodienoic acid: a new hexadecanoid signal in the jasmonate family
    • Weber H., Vick B.A., and Farmer E.E. Dinor-oxo-phytodienoic acid: a new hexadecanoid signal in the jasmonate family. Proc. Natl. Acad. Sci. USA 94 (1997) 10473-10478
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10473-10478
    • Weber, H.1    Vick, B.A.2    Farmer, E.E.3
  • 77
    • 0003357909 scopus 로고    scopus 로고
    • Cytochromes P450
    • American Society of Plant Biologists, Rockville, MD. doi:10.1199/tab.002
    • Werck-Reichhart, D., Bak, S., Paquette, S., 2002. Cytochromes P450. In: The Arabidopsis Book. American Society of Plant Biologists, Rockville, MD. doi:10.1199/tab.002.
    • (2002) The Arabidopsis Book
    • Werck-Reichhart, D.1    Bak, S.2    Paquette, S.3
  • 78
    • 33845877465 scopus 로고    scopus 로고
    • Preparative enzymatic solid phase synthesis of cis(+)-12-oxo-phytodienoic acid - physical interaction of AOS and AOC is not necessary
    • Zerbe P., Weiler E.W., and Schaller F. Preparative enzymatic solid phase synthesis of cis(+)-12-oxo-phytodienoic acid - physical interaction of AOS and AOC is not necessary. Phytochemistry 68 (2007) 229-236
    • (2007) Phytochemistry , vol.68 , pp. 229-236
    • Zerbe, P.1    Weiler, E.W.2    Schaller, F.3
  • 79
    • 0031403379 scopus 로고    scopus 로고
    • Purification and characterization of allene oxide cyclase from dry corn seeds
    • Ziegler J., Hamberg M., Miersch O., and Parthier B. Purification and characterization of allene oxide cyclase from dry corn seeds. Plant Physiol. 114 (1997) 565-573
    • (1997) Plant Physiol. , vol.114 , pp. 565-573
    • Ziegler, J.1    Hamberg, M.2    Miersch, O.3    Parthier, B.4
  • 80
    • 0032700710 scopus 로고    scopus 로고
    • On the specificity of allene oxide cyclase
    • Ziegler J., Wasternack C., and Hamberg M. On the specificity of allene oxide cyclase. Lipids 34 (1999) 1005-1015
    • (1999) Lipids , vol.34 , pp. 1005-1015
    • Ziegler, J.1    Wasternack, C.2    Hamberg, M.3
  • 81
    • 0034705429 scopus 로고    scopus 로고
    • Molecular cloning of allene oxide cyclase. The enzyme establishing the stereochemistry of octadecanoids and jasmonates
    • Ziegler J., Stenzel I., Hause B., Maucher H., Hamberg M., Grimm R., Ganal M., and Wasternack C. Molecular cloning of allene oxide cyclase. The enzyme establishing the stereochemistry of octadecanoids and jasmonates. J. Biol. Chem. 275 (2000) 19132-19138
    • (2000) J. Biol. Chem. , vol.275 , pp. 19132-19138
    • Ziegler, J.1    Stenzel, I.2    Hause, B.3    Maucher, H.4    Hamberg, M.5    Grimm, R.6    Ganal, M.7    Wasternack, C.8
  • 82
    • 0035201037 scopus 로고    scopus 로고
    • The Arabidopsis pxa1 mutant is defective in an ATP-binding cassette transporter-like protein required for peroxisomal fatty acid β-oxidation
    • Zolman B.K., Silva I.D., and Bartel B. The Arabidopsis pxa1 mutant is defective in an ATP-binding cassette transporter-like protein required for peroxisomal fatty acid β-oxidation. Plant Physiol. 127 (2001) 1266-1278
    • (2001) Plant Physiol. , vol.127 , pp. 1266-1278
    • Zolman, B.K.1    Silva, I.D.2    Bartel, B.3


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