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Volumn 13, Issue 1, 2017, Pages 69-74

Elucidation of gibberellin biosynthesis in bacteria reveals convergent evolution

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME P450; FERREDOXIN; GIBBERELLIN; KAURENOIC ACID;

EID: 84995376464     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.2232     Document Type: Article
Times cited : (95)

References (60)
  • 1
    • 84944539463 scopus 로고    scopus 로고
    • A century of gibberellin research
    • Hedden, P., Sponsel, V. A century of gibberellin research. J. Plant Growth Regul. 34, 740-760 (2015).
    • (2015) J. Plant Growth Regul. , vol.34 , pp. 740-760
    • Hedden, P.1    Sponsel, V.2
  • 2
    • 84860817547 scopus 로고    scopus 로고
    • Gibberellin biosynthesis and its regulation
    • Hedden, P., Thomas, S.G. Gibberellin biosynthesis and its regulation. Biochem. J. 444, 11-25 (2012).
    • (2012) Biochem. J. , vol.444 , pp. 11-25
    • Hedden, P.1    Thomas, S.G.2
  • 3
    • 60449092387 scopus 로고    scopus 로고
    • Role of plant hormones in plant defence responses
    • Bari, R., Jones, J.D.G. Role of plant hormones in plant defence responses. Plant Mol. Biol. 69, 473-488 (2009).
    • (2009) Plant Mol. Biol. , vol.69 , pp. 473-488
    • Bari, R.1    Jones, J.D.G.2
  • 5
    • 0033566192 scopus 로고    scopus 로고
    • Green revolution' genes encode mutant gibberellin response modulators
    • Peng, J., et al. 'Green revolution' genes encode mutant gibberellin response modulators. Nature 400, 256-261 (1999).
    • (1999) Nature , vol.400 , pp. 256-261
    • Peng, J.1
  • 6
    • 0037129230 scopus 로고    scopus 로고
    • Green revolution: A mutant gibberellin-synthesis gene in rice
    • Sasaki, A., et al. Green revolution: a mutant gibberellin-synthesis gene in rice. Nature 416, 701-702 (2002).
    • (2002) Nature , vol.416 , pp. 701-702
    • Sasaki, A.1
  • 7
    • 70350734276 scopus 로고    scopus 로고
    • Diversity regulation, and evolution of the gibberellin biosynthetic pathway in fungi compared to plants and bacteria
    • Bömke, C., Tudzynski, B. Diversity, regulation, and evolution of the gibberellin biosynthetic pathway in fungi compared to plants and bacteria. Phytochemistry 70, 1876-1893 (2009).
    • (2009) Phytochemistry , vol.70 , pp. 1876-1893
    • Bömke, C.1    Tudzynski, B.2
  • 8
    • 0035738917 scopus 로고    scopus 로고
    • Occurrence of gibberellins in vascular plants, fungi, and bacteria
    • MacMillan, J. Occurrence of gibberellins in vascular plants, fungi, and bacteria. J. Plant Growth Regul. 20, 387-442 (2001).
    • (2001) J. Plant Growth Regul. , vol.20 , pp. 387-442
    • MacMillan, J.1
  • 9
    • 15244355141 scopus 로고    scopus 로고
    • Gibberellin biosynthesis in fungi: Genes, enzymes, evolution, and impact on biotechnology
    • Tudzynski, B. Gibberellin biosynthesis in fungi: genes, enzymes, evolution, and impact on biotechnology. Appl. Microbiol. Biotechnol. 66, 597-611 (2005).
    • (2005) Appl. Microbiol. Biotechnol. , vol.66 , pp. 597-611
    • Tudzynski, B.1
  • 10
    • 58149507674 scopus 로고    scopus 로고
    • Gibberellin biosynthesis in bacteria: Separate ent-copalyl diphosphate and ent-kaurene synthases in Bradyrhizobium japonicum
    • Morrone, D., et al. Gibberellin biosynthesis in bacteria: separate ent-copalyl diphosphate and ent-kaurene synthases in Bradyrhizobium japonicum. FEBS Lett. 583, 475-480 (2009).
    • (2009) FEBS Lett. , vol.583 , pp. 475-480
    • Morrone, D.1
  • 11
    • 84873154752 scopus 로고    scopus 로고
    • CYP714B1 and CYP714B2 encode gibberellin 13-oxidases that reduce gibberellin activity in rice
    • Magome, H., et al. CYP714B1 and CYP714B2 encode gibberellin 13-oxidases that reduce gibberellin activity in rice. Proc. Natl. Acad. Sci. USA 110, 1947-1952 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 1947-1952
    • Magome, H.1
  • 12
    • 84867137481 scopus 로고    scopus 로고
    • Characterization of the fungal gibberellin desaturase as a 2-oxoglutarate-dependent dioxygenase and its utilization for enhancing plant growth
    • Bhattacharya, A., et al. Characterization of the fungal gibberellin desaturase as a 2-oxoglutarate-dependent dioxygenase and its utilization for enhancing plant growth. Plant Physiol. 160, 837-845 (2012).
    • (2012) Plant Physiol. , vol.160 , pp. 837-845
    • Bhattacharya, A.1
  • 14
    • 0000231011 scopus 로고
    • Production of gibberellins and indole-3-acetic acid by Rhizobium phaseoli in relation to nodulation of Phaseolus vulgaris roots
    • Atzorn, R., Crozier, A., Wheeler, C.T., Sandberg, G. Production of gibberellins and indole-3-acetic acid by Rhizobium phaseoli in relation to nodulation of Phaseolus vulgaris roots. Planta 175, 532-538 (1988).
    • (1988) Planta , vol.175 , pp. 532-538
    • Atzorn, R.1    Crozier, A.2    Wheeler, C.T.3    Sandberg, G.4
  • 15
    • 84878766926 scopus 로고    scopus 로고
    • Polyphasic evidence supporting the reclassification of Bradyrhizobium japonicum group Ia strains as Bradyrhizobium diazoefficiens sp
    • Delamuta, J.R.M., et al. Polyphasic evidence supporting the reclassification of Bradyrhizobium japonicum group Ia strains as Bradyrhizobium diazoefficiens sp. nov. Int. J. Syst. Evol. Microbiol. 63, 3342-3351 (2013).
    • (2013) Nov. Int. J. Syst. Evol. Microbiol. , vol.63 , pp. 3342-3351
    • Delamuta, J.R.M.1
  • 16
    • 0027372515 scopus 로고
    • Cloning and mutagenesis of a cytochrome P-450 locus from Bradyrhizobium japonicum that is expressed anaerobically and symbiotically
    • Tully, R.E., Keister, D.L. Cloning and mutagenesis of a cytochrome P-450 locus from Bradyrhizobium japonicum that is expressed anaerobically and symbiotically. Appl. Environ. Microbiol. 59, 4136-4142 (1993).
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 4136-4142
    • Tully, R.E.1    Keister, D.L.2
  • 17
    • 0032500154 scopus 로고    scopus 로고
    • Identification and sequencing of a cytochrome P450 gene cluster from Bradyrhizobium japonicum
    • Tully, R.E., van Berkum, P., Lovins, K.W., Keister, D.L. Identification and sequencing of a cytochrome P450 gene cluster from Bradyrhizobium japonicum. Biochim. Biophys. Acta 1398, 243-255 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1398 , pp. 243-255
    • Tully, R.E.1    Van Berkum, P.2    Lovins, K.W.3    Keister, D.L.4
  • 19
    • 84892919074 scopus 로고    scopus 로고
    • Gibberellin oxidase activities in Bradyrhizobium japonicum bacteroids
    • Méndez, C., et al. Gibberellin oxidase activities in Bradyrhizobium japonicum bacteroids. Phytochemistry 98, 101-109 (2014).
    • (2014) Phytochemistry , vol.98 , pp. 101-109
    • Méndez, C.1
  • 20
    • 84890279702 scopus 로고    scopus 로고
    • Functional conservation of the capacity for ent-kaurene biosynthesis and an associated operon in certain rhizobia
    • Hershey, D.M., Lu, X., Zi, J., Peters, R.J. Functional conservation of the capacity for ent-kaurene biosynthesis and an associated operon in certain rhizobia. J. Bacteriol. 196, 100-106 (2014).
    • (2014) J. Bacteriol. , vol.196 , pp. 100-106
    • Hershey, D.M.1    Lu, X.2    Zi, J.3    Peters, R.J.4
  • 21
    • 0035958746 scopus 로고    scopus 로고
    • The composite genome of the legume symbiont Sinorhizobium meliloti
    • Galibert, F., et al. The composite genome of the legume symbiont Sinorhizobium meliloti. Science 293, 668-672 (2001).
    • (2001) Science , vol.293 , pp. 668-672
    • Galibert, F.1
  • 22
    • 33846473252 scopus 로고    scopus 로고
    • Cytochrome P450 systems-biological variations of electron transport chains
    • Hannemann, F., Bichet, A., Ewen, K.M., Bernhardt, R. Cytochrome P450 systems-biological variations of electron transport chains. Biochim. Biophys. Acta 1770, 330-344 (2007).
    • (2007) Biochim. Biophys. Acta , vol.1770 , pp. 330-344
    • Hannemann, F.1    Bichet, A.2    Ewen, K.M.3    Bernhardt, R.4
  • 23
    • 0028289983 scopus 로고
    • Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: Selection of defined deletions in the chromosome of Corynebacterium glutamicum
    • Schäfer, A., et al. Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: selection of defined deletions in the chromosome of Corynebacterium glutamicum. Gene 145, 69-73 (1994).
    • (1994) Gene , vol.145 , pp. 69-73
    • Schäfer, A.1
  • 24
    • 0037398045 scopus 로고    scopus 로고
    • Application of crossover-PCR-mediated deletion-insertion mutagenesis to analysis of the bdhA-xdhA2-xdhB2 mixed-function operon of Sinorhizobium meliloti
    • Sukdeo, N., Charles, T.C. Application of crossover-PCR-mediated deletion-insertion mutagenesis to analysis of the bdhA-xdhA2-xdhB2 mixed-function operon of Sinorhizobium meliloti. Arch. Microbiol. 179, 301-304 (2003).
    • (2003) Arch. Microbiol. , vol.179 , pp. 301-304
    • Sukdeo, N.1    Charles, T.C.2
  • 25
    • 0001387037 scopus 로고
    • The chemistry of gibberellins: An overview
    • Mander, L.N. The chemistry of gibberellins: an overview. Chem. Rev. 92, 573-612 (1992).
    • (1992) Chem. Rev. , vol.92 , pp. 573-612
    • Mander, L.N.1
  • 26
    • 0037020824 scopus 로고    scopus 로고
    • Construction of cyclopentyl units by ring contraction reactions
    • Silva, L.F. Construction of cyclopentyl units by ring contraction reactions. Tetrahedron 58, 9137-9161 (2002).
    • (2002) Tetrahedron , vol.58 , pp. 9137-9161
    • Silva, L.F.1
  • 27
    • 84896916642 scopus 로고    scopus 로고
    • Labelling studies on the biosynthesis of terpenes in Fusarium fujikuroi
    • Citron, C.A., Brock, N.L., Tudzynski, B., Dickschat, J.S. Labelling studies on the biosynthesis of terpenes in Fusarium fujikuroi. Chem. Commun. (Camb.) 50, 5224-5226 (2014).
    • (2014) Chem. Commun. (Camb.) , vol.50 , pp. 5224-5226
    • Citron, C.A.1    Brock, N.L.2    Tudzynski, B.3    Dickschat, J.S.4
  • 28
    • 0035852752 scopus 로고    scopus 로고
    • The CYP88A cytochrome P450, ent-kaurenoic acid oxidase, catalyzes three steps of the gibberellin biosynthesis pathway
    • Helliwell, C.A., Chandler, P.M., Poole, A., Dennis, E.S., Peacock, W.J. The CYP88A cytochrome P450, ent-kaurenoic acid oxidase, catalyzes three steps of the gibberellin biosynthesis pathway. Proc. Natl. Acad. Sci. USA 98, 2065-2070 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2065-2070
    • Helliwell, C.A.1    Chandler, P.M.2    Poole, A.3    Dennis, E.S.4    Peacock, W.J.5
  • 29
    • 0035826779 scopus 로고    scopus 로고
    • The P450-1 gene of Gibberella fujikuroi encodes a multifunctional enzyme in gibberellin biosynthesis
    • Rojas, M.C., Hedden, P., Gaskin, P., Tudzynski, B. The P450-1 gene of Gibberella fujikuroi encodes a multifunctional enzyme in gibberellin biosynthesis. Proc. Natl. Acad. Sci. USA 98, 5838-5843 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5838-5843
    • Rojas, M.C.1    Hedden, P.2    Gaskin, P.3    Tudzynski, B.4
  • 30
    • 13544263331 scopus 로고    scopus 로고
    • Identification of intermediates and enzymes involved in the early steps of artemisinin biosynthesis in Artemisia annua
    • Bertea, C.M., et al. Identification of intermediates and enzymes involved in the early steps of artemisinin biosynthesis in Artemisia annua. Planta Med. 71, 40-47 (2005).
    • (2005) Planta Med. , vol.71 , pp. 40-47
    • Bertea, C.M.1
  • 31
    • 68149089486 scopus 로고    scopus 로고
    • Molecular cloning of an aldehyde dehydrogenase implicated in artemisinin biosynthesis in Artemisia annua
    • Teoh, K.H., Polichuk, D.R., Reed, D.W., Covello, P.S. Molecular cloning of an aldehyde dehydrogenase implicated in artemisinin biosynthesis in Artemisia annua. Botany 87, 635-642 (2009).
    • (2009) Botany , vol.87 , pp. 635-642
    • Teoh, K.H.1    Polichuk, D.R.2    Reed, D.W.3    Covello, P.S.4
  • 32
    • 84964816641 scopus 로고    scopus 로고
    • Characterization of a unique pathway for 4-cresol catabolism initiated by phosphorylation in Corynebacterium glutamicum
    • Du, L., et al. Characterization of a unique pathway for 4-cresol catabolism initiated by phosphorylation in Corynebacterium glutamicum. J. Biol. Chem. 291, 6583-6594 (2016).
    • (2016) J. Biol. Chem. , vol.291 , pp. 6583-6594
    • Du, L.1
  • 33
    • 77955822715 scopus 로고    scopus 로고
    • Diterpene cyclases and the nature of the isoprene fold
    • Cao, R., et al. Diterpene cyclases and the nature of the isoprene fold. Proteins 78, 2417-2432 (2010).
    • (2010) Proteins , vol.78 , pp. 2417-2432
    • Cao, R.1
  • 34
    • 84923261278 scopus 로고    scopus 로고
    • Structure, function and inhibition of ent-kaurene synthase from Bradyrhizobium japonicum
    • Liu, W., et al. Structure, function and inhibition of ent-kaurene synthase from Bradyrhizobium japonicum. Sci. Rep. 4, 6214 (2014).
    • (2014) Sci. Rep. , vol.4 , pp. 6214
    • Liu, W.1
  • 35
    • 0033199227 scopus 로고    scopus 로고
    • Cytochrome P450 and the individuality of species
    • Nelson, D.R. Cytochrome P450 and the individuality of species. Arch. Biochem. Biophys. 369, 1-10 (1999).
    • (1999) Arch. Biochem. Biophys. , vol.369 , pp. 1-10
    • Nelson, D.R.1
  • 36
    • 0030996327 scopus 로고    scopus 로고
    • Cloning gibberellin dioxygenase genes from pumpkin endosperm by heterologous expression of enzyme activities in Escherichia coli
    • Lange, T. Cloning gibberellin dioxygenase genes from pumpkin endosperm by heterologous expression of enzyme activities in Escherichia coli. Proc. Natl. Acad. Sci. USA 94, 6553-6558 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6553-6558
    • Lange, T.1
  • 37
    • 79955058143 scopus 로고    scopus 로고
    • Convergent evolution in biosynthesis of cyanogenic defence compounds in plants and insects
    • Jensen, N.B., et al. Convergent evolution in biosynthesis of cyanogenic defence compounds in plants and insects. Nat. Commun. 2, 273 (2011).
    • (2011) Nat. Commun. , vol.2 , pp. 273
    • Jensen, N.B.1
  • 39
    • 80755176872 scopus 로고    scopus 로고
    • Semipinacol rearrangement in natural product synthesis
    • Song, Z.L., Fan, C.A., Tu, Y.Q. Semipinacol rearrangement in natural product synthesis. Chem. Rev. 111, 7523-7556 (2011).
    • (2011) Chem. Rev. , vol.111 , pp. 7523-7556
    • Song, Z.L.1    Fan, C.A.2    Tu, Y.Q.3
  • 40
    • 77954259799 scopus 로고    scopus 로고
    • Endogenous diterpenes derived from ent-kaurene, a common gibberellin precursor, regulate protonema differentiation of the moss Physcomitrella patens
    • Hayashi, K., et al. Endogenous diterpenes derived from ent-kaurene, a common gibberellin precursor, regulate protonema differentiation of the moss Physcomitrella patens. Plant Physiol. 153, 1085-1097 (2010).
    • (2010) Plant Physiol. , vol.153 , pp. 1085-1097
    • Hayashi, K.1
  • 41
    • 43049142587 scopus 로고    scopus 로고
    • DELLAs control plant immune responses by modulating the balance of jasmonic acid and salicylic acid signaling
    • Navarro, L., et al. DELLAs control plant immune responses by modulating the balance of jasmonic acid and salicylic acid signaling. Curr. Biol. 18, 650-655 (2008).
    • (2008) Curr. Biol. , vol.18 , pp. 650-655
    • Navarro, L.1
  • 42
    • 60449096691 scopus 로고    scopus 로고
    • Altered disease development in the eui mutants and Eui overexpressors indicates that gibberellins negatively regulate rice basal disease resistance
    • Yang, D.L., et al. Altered disease development in the eui mutants and Eui overexpressors indicates that gibberellins negatively regulate rice basal disease resistance. Mol. Plant 1, 528-537 (2008).
    • (2008) Mol. Plant , vol.1 , pp. 528-537
    • Yang, D.L.1
  • 43
    • 84879514195 scopus 로고    scopus 로고
    • Deciphering the cryptic genome: Genome-wide analyses of the rice pathogen Fusarium fujikuroi reveal complex regulation of secondary metabolism and novel metabolites
    • Wiemann, P., et al. Deciphering the cryptic genome: genome-wide analyses of the rice pathogen Fusarium fujikuroi reveal complex regulation of secondary metabolism and novel metabolites. PLoS Pathog. 9, e1003475 (2013).
    • (2013) PLoS Pathog. , vol.9 , pp. 1003475
    • Wiemann, P.1
  • 44
    • 84923291490 scopus 로고    scopus 로고
    • An ent-kaurene-derived diterpenoid virulence factor from Xanthomonas oryzae pv. Oryzicola
    • Lu, X., Hershey, D.M., Wang, L., Bogdanove, A.J., Peters, R.J. An ent-kaurene-derived diterpenoid virulence factor from Xanthomonas oryzae pv. oryzicola. New Phytol. 206, 295-302 (2015).
    • (2015) New Phytol. , vol.206 , pp. 295-302
    • Lu, X.1    Hershey, D.M.2    Wang, L.3    Bogdanove, A.J.4    Peters, R.J.5
  • 45
    • 77952919225 scopus 로고    scopus 로고
    • Plants versus pathogens: An evolutionary arms race
    • Anderson, J.P., et al. Plants versus pathogens: an evolutionary arms race. Funct. Plant Biol. 37, 499-512 (2010).
    • (2010) Funct. Plant Biol. , vol.37 , pp. 499-512
    • Anderson, J.P.1
  • 46
    • 0021013060 scopus 로고
    • Physical and genetic characterization of Rhizobium meliloti symbiotic mutants
    • Buikema, W.J., et al. Physical and genetic characterization of Rhizobium meliloti symbiotic mutants. J. Mol. Appl. Genet. 2, 249-260 (1983).
    • (1983) J. Mol. Appl. Genet. , vol.2 , pp. 249-260
    • Buikema, W.J.1
  • 47
    • 84980243155 scopus 로고
    • Relationships amongst the fast-growing rhizobia of Lablab purpureus, Leucaena leucocephala, Mimosa spp., Acacia farnesiana and Sesbania grandiflora and their affinities with other rhizobial groups
    • Trinick, M.J. Relationships amongst the fast-growing rhizobia of Lablab purpureus, Leucaena leucocephala, Mimosa spp., Acacia farnesiana and Sesbania grandiflora and their affinities with other rhizobial groups. J. Appl. Bacteriol. 49, 39-53 (1980).
    • (1980) J. Appl. Bacteriol. , vol.49 , pp. 39-53
    • Trinick, M.J.1
  • 48
    • 0033529797 scopus 로고    scopus 로고
    • Characterization and catalytic properties of the sterol 14?-demethylase from Mycobacterium tuberculosis
    • Bellamine, A., Mangla, A.T., Nes, W.D., Waterman, M.R. Characterization and catalytic properties of the sterol 14?-demethylase from Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 96, 8937-8942 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8937-8942
    • Bellamine, A.1    Mangla, A.T.2    Nes, W.D.3    Waterman, M.R.4
  • 49
    • 33847674077 scopus 로고    scopus 로고
    • Pentalenolactone biosyn thesis: Molecular cloning and assignment of biochemical function to PtlF, a short-chain dehydrogenase from Streptomyces avermitilis, and identification of a new biosynthetic intermediate
    • You, Z., Omura, S., Ikeda, H., Cane, D.E. Pentalenolactone biosynthesis: molecular cloning and assignment of biochemical function to PtlF, a short-chain dehydrogenase from Streptomyces avermitilis, and identification of a new biosynthetic intermediate. Arch. Biochem. Biophys. 459, 233-240 (2007).
    • (2007) Arch. Biochem. Biophys. , vol.459 , pp. 233-240
    • You, Z.1    Omura, S.2    Ikeda, H.3    Cane, D.E.4
  • 50
    • 84866309710 scopus 로고    scopus 로고
    • Increased production of the exopolysaccharide succinoglycan enhances Sinorhizobium meliloti 1021 symbiosis with the host plant Medicago truncatula
    • Jones, K.M. Increased production of the exopolysaccharide succinoglycan enhances Sinorhizobium meliloti 1021 symbiosis with the host plant Medicago truncatula. J. Bacteriol. 194, 4322-4331 (2012).
    • (2012) J. Bacteriol. , vol.194 , pp. 4322-4331
    • Jones, K.M.1
  • 51
    • 0021050914 scopus 로고
    • Tetracycline resistance determined by pBR322 is mediated by one polypeptide
    • Backman, K., Boyer, H.W. Tetracycline resistance determined by pBR322 is mediated by one polypeptide. Gene 26, 197-203 (1983).
    • (1983) Gene , vol.26 , pp. 197-203
    • Backman, K.1    Boyer, H.W.2
  • 52
    • 0022474397 scopus 로고
    • Second symbiotic megaplasmid in Rhizobium meliloti carrying exopolysaccharide and thiamine synthesis genes
    • Finan, T.M., Kunkel, B., De Vos, G.F., Signer, E.R. Second symbiotic megaplasmid in Rhizobium meliloti carrying exopolysaccharide and thiamine synthesis genes. J. Bacteriol. 167, 66-72 (1986).
    • (1986) J. Bacteriol. , vol.167 , pp. 66-72
    • Finan, T.M.1    Kunkel, B.2    De Vos, G.F.3    Signer, E.R.4
  • 53
    • 76849089864 scopus 로고    scopus 로고
    • Increasing diterpene yield with a modular metabolic engineering system in E. Coli: Comparison of MEV and MEP isoprenoid precursor pathway engineering
    • Morrone, D., et al. Increasing diterpene yield with a modular metabolic engineering system in E. coli: comparison of MEV and MEP isoprenoid precursor pathway engineering. Appl. Microbiol. Biotechnol. 85, 1893-1906 (2010).
    • (2010) Appl. Microbiol. Biotechnol. , vol.85 , pp. 1893-1906
    • Morrone, D.1
  • 54
    • 0002775216 scopus 로고    scopus 로고
    • Stereochemistry of the oxidation of gibberellin 20-alcohols, GA15 and GA44, to 20-aldehydes by gibberellin 20-oxidases
    • Ward, J.L., et al. Stereochemistry of the oxidation of gibberellin 20-alcohols, GA15 and GA44, to 20-aldehydes by gibberellin 20-oxidases. Chem. Commun. (Camb.) 13-14 (1997).
    • (1997) Chem. Commun. (Camb.) , pp. 13-14
    • Ward, J.L.1
  • 55
    • 0001459408 scopus 로고
    • The biosynthesis of all major pea gibberellins in a cell-free system from Pisum sativum
    • Kamiya, Y., Graebe, J.E. The biosynthesis of all major pea gibberellins in a cell-free system from Pisum sativum. Phytochemistry 22, 681-689 (1983).
    • (1983) Phytochemistry , vol.22 , pp. 681-689
    • Kamiya, Y.1    Graebe, J.E.2
  • 56
    • 84866170203 scopus 로고    scopus 로고
    • Biotechnological production of caffeic acid by bacterial cytochrome P450 CYP199A2
    • Furuya, T., Arai, Y., Kino, K. Biotechnological production of caffeic acid by bacterial cytochrome P450 CYP199A2. Appl. Environ. Microbiol. 78, 6087-6094 (2012).
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 6087-6094
    • Furuya, T.1    Arai, Y.2    Kino, K.3
  • 57
    • 2142658159 scopus 로고
    • Combined gas chromatography-mass spectrometry of the methyl esters of gibberellins A1 to A24 and their trimethylsilyl ethers
    • Binks, R., MacMillan, J., Pryce, R.J. Combined gas chromatography-mass spectrometry of the methyl esters of gibberellins A1 to A24 and their trimethylsilyl ethers. Phytochemistry 8, 271-284 (1969).
    • (1969) Phytochemistry , vol.8 , pp. 271-284
    • Binks, R.1    MacMillan, J.2    Pryce, R.J.3
  • 58
    • 0001016397 scopus 로고
    • Biosynthesis of gibberellins A12, A15, A24, A36, and A37 by a cell-free system from Cucurbita maxima
    • Graebe, J.E., Hedden, P., Gaskin, P., MacMillan, J. Biosynthesis of gibberellins A12, A15, A24, A36, and A37 by a cell-free system from Cucurbita maxima. Phytochemistry 13, 1433-1440 (1974).
    • (1974) Phytochemistry , vol.13 , pp. 1433-1440
    • Graebe, J.E.1    Hedden, P.2    Gaskin, P.3    MacMillan, J.4
  • 59
    • 0035830948 scopus 로고    scopus 로고
    • Monooxygenases involved in GA12 and GA14 synthesis in Gibberella fujikuroi
    • Urrutia, O., Hedden, P., Rojas, M.C. Monooxygenases involved in GA12 and GA14 synthesis in Gibberella fujikuroi. Phytochemistry 56, 505-511 (2001).
    • (2001) Phytochemistry , vol.56 , pp. 505-511
    • Urrutia, O.1    Hedden, P.2    Rojas, M.C.3
  • 60
    • 38349098007 scopus 로고    scopus 로고
    • Influence of electron transport proteins on the reactions catalyzed by Fusarium fujikuroi gibberellin monooxygenases
    • Troncoso, C., Cárcamo, J., Hedden, P., Tudzynski, B., Rojas, M.C. Influence of electron transport proteins on the reactions catalyzed by Fusarium fujikuroi gibberellin monooxygenases. Phytochemistry 69, 672-683 (2008).
    • (2008) Phytochemistry , vol.69 , pp. 672-683
    • Troncoso, C.1    Cárcamo, J.2    Hedden, P.3    Tudzynski, B.4    Rojas, M.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.