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Volumn 14, Issue 7, 2013, Pages 13626-13644

Early phenylpropanoid biosynthetic steps in Cannabis sativa: Link between genes and metabolites

Author keywords

4 coumarate; Cannabis sativa; Chalcone synthase; Cinnamic acid 4 hydroxylase; CoA ligase; Expression analysis; NMR metabolic profiling; Phenylalanine ammonia lyase; Phenylpropanoid; Secondary metabolism

Indexed keywords

CAFFEIC ACID PHENETHYL ESTER; CANNABIS; CATECHOL METHYLTRANSFERASE; CHALCONE SYNTHASE; CINNAMATE 4 MONOOXYGENASE; COMPLEMENTARY DNA; FLAVONOID; LIGNIN; PARA COUMARIC ACID; PHENYLALANINE AMMONIA LYASE; VEGETABLE PROTEIN;

EID: 84879989628     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms140713626     Document Type: Article
Times cited : (33)

References (80)
  • 2
    • 84863207024 scopus 로고    scopus 로고
    • Variation in physical and mechanical properties of hemp stalk fibers along height of stem
    • Li, X.; Wang, S.; Du, G.; Wu, Z.; Meng, Y. Variation in physical and mechanical properties of hemp stalk fibers along height of stem. Ind. Crops Prod. 2013, 42, 344-348.
    • (2013) Ind. Crops Prod , vol.42 , pp. 344-348
    • Li, X.1    Wang, S.2    Du, G.3    Wu, Z.4    Meng, Y.5
  • 3
    • 33645735834 scopus 로고    scopus 로고
    • Safety issues concerning the medical use of cannabis and cannabinoids
    • Ware, M.A.; Tawfik, V.L. Safety issues concerning the medical use of cannabis and cannabinoids. Pain Res. Manag. 2005, 10, 31A-37A.
    • (2005) Pain Res. Manag , vol.10
    • Ware, M.A.1    Tawfik, V.L.2
  • 5
    • 34848836633 scopus 로고    scopus 로고
    • Quality of chemically modified hemp fibres
    • Kostic, M.; Pejic, B.; Skundric, P. Quality of chemically modified hemp fibres. Biorsource Technol. 2008, 99, 94-99.
    • (2008) Biorsource Technol , vol.99 , pp. 94-99
    • Kostic, M.1    Pejic, B.2    Skundric, P.3
  • 7
    • 84864419262 scopus 로고    scopus 로고
    • The hexanoyl-CoA precursor for cannabinoid biosynthesis is formed by an acyl-activating enzyme in Cannabis sativa trichomes
    • Stout, J.M.; Boubakir, Z.; Ambrose, S.J.; Purves, R.W.; Page, J.E. The hexanoyl-CoA precursor for cannabinoid biosynthesis is formed by an acyl-activating enzyme in Cannabis sativa trichomes. Plant J. 2012, 71, 353-365.
    • (2012) Plant J , vol.71 , pp. 353-365
    • Stout, J.M.1    Boubakir, Z.2    Ambrose, S.J.3    Purves, R.W.4    Page, J.E.5
  • 8
    • 33746496150 scopus 로고    scopus 로고
    • Significance of flavonoids in plant reistance: A review
    • Treutter, D. Significance of flavonoids in plant reistance: A review. Env. Chem. Lett. 2006, 4, 147-157.
    • (2006) Env. Chem. Lett , vol.4 , pp. 147-157
    • Treutter, D.1
  • 9
    • 76549093442 scopus 로고    scopus 로고
    • Phenylpropanoid biosynthesis
    • Vogt, T. Phenylpropanoid biosynthesis. Mol. Plant 2010, 3, 2-20.
    • (2010) Mol. Plant , vol.3 , pp. 2-20
    • Vogt, T.1
  • 11
    • 73049125969 scopus 로고
    • The metabolism of aromatic compounds in higher plants. IV. Purification and properties of the phenylalanine deaminase of Hordeum vulgare
    • Koukol, J.; Conn, E.E. The metabolism of aromatic compounds in higher plants. IV. Purification and properties of the phenylalanine deaminase of Hordeum vulgare. J. Biol. Chem. 1961, 236, 2692-2698.
    • (1961) J. Biol. Chem , vol.236 , pp. 2692-2698
    • Koukol, J.1    Conn, E.E.2
  • 12
    • 0016794641 scopus 로고
    • A model of closely assembled consecutive enzymes on membranes: Formation of hydroxycinnamic acids from L-phenylalanine on thylakoids of Dunaliella marina
    • Czichi, U.; Kindi, H. A model of closely assembled consecutive enzymes on membranes: Formation of hydroxycinnamic acids from L-phenylalanine on thylakoids of Dunaliella marina. Hoppe Seylers. Z Physiol. Chem. 1975, 356, 475-485.
    • (1975) Hoppe Seylers. Z Physiol. Chem , vol.356 , pp. 475-485
    • Czichi, U.1    Kindi, H.2
  • 13
    • 0001463337 scopus 로고
    • Phenylalanine ammonia lyase
    • Camm, E.L.; Towers, G.H.N. Phenylalanine ammonia lyase. Phytochemistry 1973, 12, 961-973.
    • (1973) Phytochemistry , vol.12 , pp. 961-973
    • Camm, E.L.1    Towers, G.H.N.2
  • 14
    • 1842310167 scopus 로고
    • Taxonomic distribution of ammonia lyases for L-phenylalanine and L-tyrosine in relation to lignification
    • Young, M.R.; Towers, G.H.; Neish, A.C. Taxonomic distribution of ammonia lyases for L-phenylalanine and L-tyrosine in relation to lignification. Can. J. Bot. 1966, 44, 341-349.
    • (1966) Can. J. Bot , vol.44 , pp. 341-349
    • Young, M.R.1    Towers, G.H.2    Neish, A.C.3
  • 15
    • 0011270345 scopus 로고
    • Phenylalanine and tyrosine ammonia lyase activity in some Basidiomycetes
    • Bandoni, R.J.; Moore, K.; Subba Rao, P.V.; Towers, G.H. Phenylalanine and tyrosine ammonia lyase activity in some Basidiomycetes. Phytochemistry 1968, 7, 205-207.
    • (1968) Phytochemistry , vol.7 , pp. 205-207
    • Bandoni, R.J.1    Moore, K.2    Subba Rao, P.V.3    Towers, G.H.4
  • 16
    • 0015217702 scopus 로고
    • Yeast phenylalanine ammonia lyase: Purification, properties, and the identification of catalytically essential dehydroalanine
    • Hodgens, D.S. Yeast phenylalanine ammonia lyase: Purification, properties, and the identification of catalytically essential dehydroalanine. J. Biol. Chem. 1971, 246, 2977-2985.
    • (1971) J. Biol. Chem , vol.246 , pp. 2977-2985
    • Hodgens, D.S.1
  • 17
    • 0014777998 scopus 로고
    • Partial purification and properties of L-phenylalanine ammonia lyase from Streptomyces verticillatus
    • Emes, A.V.; Vining, L.C. Partial purification and properties of L-phenylalanine ammonia lyase from Streptomyces verticillatus. Can. J. Biochem. 1970, 48, 613-622.
    • (1970) Can. J. Biochem , vol.48 , pp. 613-622
    • Emes, A.V.1    Vining, L.C.2
  • 18
    • 57749088682 scopus 로고    scopus 로고
    • Tomato phenylalanine ammonia lyase gene family, highly redundant but strongly underutilized
    • Chang, A.; Lim, M.H.; Lee, S.W.; Robb, E.J.; Nazar, R.N. Tomato phenylalanine ammonia lyase gene family, highly redundant but strongly underutilized. J. Biol.Chem. 2008, 283, 33591-33601.
    • (2008) J. Biol.Chem , vol.283 , pp. 33591-33601
    • Chang, A.1    Lim, M.H.2    Lee, S.W.3    Robb, E.J.4    Nazar, R.N.5
  • 19
    • 0026543902 scopus 로고
    • Phenylalanine ammonia lyase in potato (Solanum tuberosum L.)
    • Joos, H.-J.; Halhbrock, K. Phenylalanine ammonia lyase in potato (Solanum tuberosum L.). Eur. J. Biochem. 1992, 204, 621-629.
    • (1992) Eur. J. Biochem , vol.204 , pp. 621-629
    • Joos, H.-J.1    Halhbrock, K.2
  • 20
    • 84866950529 scopus 로고    scopus 로고
    • Multiple tandem duplication of the phenylalanine ammonia lyase genes in Cucumis
    • Shang, Q.-M.; Li, L.; Dong, C.-J. Multiple tandem duplication of the phenylalanine ammonia lyase genes in Cucumis. sativus L. Planta 2012, 236, 1093-1105.
    • (2012) Sativus L. Planta , vol.236 , pp. 1093-1105
    • Shang, Q.-M.1    Li, L.2    Dong, C.-J.3
  • 21
    • 50449102086 scopus 로고    scopus 로고
    • Differential expression of four Arabidopsis PAL genes; PAL1 and PAL2 have functional specialization in abiotic environmental-triggered flavonoid synthesis
    • Olsen, K.M.; Lea, U.S.; Slimestad, R.; Verheul, M.; Lillo, C. Differential expression of four Arabidopsis PAL genes; PAL1 and PAL2 have functional specialization in abiotic environmental-triggered flavonoid synthesis. J. Plant Physiol. 2008, 165, 1491-1499.
    • (2008) J. Plant Physiol , vol.165 , pp. 1491-1499
    • Olsen, K.M.1    Lea, U.S.2    Slimestad, R.3    Verheul, M.4    Lillo, C.5
  • 22
    • 84862884032 scopus 로고    scopus 로고
    • Characterization, high-resolution mapping and differential expression of three homologous PAL genes in Coffea canephora Pierre (Rubiaceae)
    • Lepelley, M.; Mahesh, V.; McCarthy, J.; Rigoreau, M.; Crouzillat, D.; Chabrillange, N.; de Kochko, A.; Campa, C. Characterization, high-resolution mapping and differential expression of three homologous PAL genes in Coffea canephora Pierre (Rubiaceae). Planta 2012, 236, 313-326.
    • (2012) Planta , vol.236 , pp. 313-326
    • Lepelley, M.1    Mahesh, V.2    McCarthy, J.3    Rigoreau, M.4    Crouzillat, D.5    Chabrillange, N.6    de Kochko, A.7    Campa, C.8
  • 24
    • 0031105968 scopus 로고    scopus 로고
    • Cinnamate-4-hydroxylase expression in Arabidopsis-Rregulation in response to development and the environment
    • Bell-Lelong, D.A.; Cusumano, J.C.; Meyer, K.; Chapple, C. Cinnamate-4-hydroxylase expression in Arabidopsis-Rregulation in response to development and the environment. Plant Physiol. 1997, 13, 729-738.
    • (1997) Plant Physiol , vol.13 , pp. 729-738
    • Bell-Lelong, D.A.1    Cusumano, J.C.2    Meyer, K.3    Chapple, C.4
  • 25
    • 0027303672 scopus 로고
    • Molecular cloning and sequencing of a cDNA encoding mung bean cytochrome-P450 (P450 C4H) possessing cinnamate-4-hydroxylase activity
    • M.; Ward, E.; Dimao, J.; Otha, D.; Ryals, J.; Sato, R. Molecular cloning and sequencing of a cDNA encoding mung bean cytochrome-P450 (P450 C4H) possessing cinnamate-4-hydroxylase activity. Biochem. Biophys. Res. Comm. 1993, 190, 875-880.
    • (1993) Biochem. Biophys. Res. Comm , vol.190 , pp. 875-880
  • 26
    • 0031105483 scopus 로고    scopus 로고
    • Isolation of a cDNA and genomic clone encoding cinnamate-4-hydroxylase from Arabidopsis and its expression manner in planta
    • Mizutani, M.; Otha, D.; Sato, R. Isolation of a cDNA and genomic clone encoding cinnamate-4-hydroxylase from Arabidopsis and its expression manner in planta. Plant Physiol. 1997, 113, 755-763.
    • (1997) Plant Physiol , vol.113 , pp. 755-763
    • Mizutani, M.1    Otha, D.2    Sato, R.3
  • 27
    • 0030268133 scopus 로고    scopus 로고
    • Isolation and analysis of cinnamic acid 4-hydroxylase homologous genes from a hybrid aspen, Populus kitatamiensis
    • Kawai, S.; Mori, A.; Shiokawa, T.; Kajita, S.; Katayama, Y.; Morohoshi, N. Isolation and analysis of cinnamic acid 4-hydroxylase homologous genes from a hybrid aspen, Populus kitatamiensis. Biosci. Biotechnol. Biochem. 1996, 60, 1586-1597.
    • (1996) Biosci. Biotechnol. Biochem , vol.60 , pp. 1586-1597
    • Kawai, S.1    Mori, A.2    Shiokawa, T.3    Kajita, S.4    Katayama, Y.5    Morohoshi, N.6
  • 28
    • 26844503174 scopus 로고    scopus 로고
    • cDNA cloning and sequence analysis of the rice cinnamate-4-hydroxylase gene, a cytochrome P450-dependent monooxygenase involved in the general phenylpropanoid pathway
    • Yang, D.H.; Chung, B.Y.; Kim, J.S.; Kim, J.H.; Yun, P.Y.; Lee, Y.K.; Lim, Y.P.; Lee, M.C. cDNA cloning and sequence analysis of the rice cinnamate-4-hydroxylase gene, a cytochrome P450-dependent monooxygenase involved in the general phenylpropanoid pathway. J. Plant Biol. 2005, 48, 311-318.
    • (2005) J. Plant Biol , vol.48 , pp. 311-318
    • Yang, D.H.1    Chung, B.Y.2    Kim, J.S.3    Kim, J.H.4    Yun, P.Y.5    Lee, Y.K.6    Lim, Y.P.7    Lee, M.C.8
  • 29
    • 0034808692 scopus 로고    scopus 로고
    • Differential expression of two cinnamate 4-hydroxylases in "Valencia" orange (Citrus sinensis Osbeck)
    • Betz, C.; McCollum, T.G.; Mayer, R.T. Differential expression of two cinnamate 4-hydroxylases in "Valencia" orange (Citrus sinensis Osbeck). Plant Mol. Biol. 2001, 46, 741-748.
    • (2001) Plant Mol. Biol , vol.46 , pp. 741-748
    • Betz, C.1    McCollum, T.G.2    Mayer, R.T.3
  • 31
    • 0031766440 scopus 로고    scopus 로고
    • Molecular genetic analysis of plant cytochrome P450-dependent monookygenases
    • Chapple, C. Molecular genetic analysis of plant cytochrome P450-dependent monookygenases. Annu. Rev. Plant Physiol. Plant mol. Biol. 1998, 46, 311-343.
    • (1998) Annu. Rev. Plant Physiol. Plant Mol. Biol , vol.46 , pp. 311-343
    • Chapple, C.1
  • 32
    • 33748944013 scopus 로고    scopus 로고
    • Multiple cis-regulatory elements regulate distinct and complex patterns of developmental and wound-induced expression of Arabidopsis thaliana 4CL gene family members
    • Soltani, B.M.; Ehlting, J.; Hamberger, B.; Dougla, C.J. Multiple cis-regulatory elements regulate distinct and complex patterns of developmental and wound-induced expression of Arabidopsis thaliana 4CL gene family members. Planta 2006, 224, 1226-1238.
    • (2006) Planta , vol.224 , pp. 1226-1238
    • Soltani, B.M.1    Ehlting, J.2    Hamberger, B.3    Dougla, C.J.4
  • 33
    • 53849144970 scopus 로고    scopus 로고
    • Identification of a 4-coumarate:CoA ligase gene family in the moss, Physcomitrella patens
    • Silber, M.V.; Meimberg, H.; Ebel, J. Identification of a 4-coumarate:CoA ligase gene family in the moss, Physcomitrella patens. Phytochemistry 2008, 69, 2449-2456.
    • (2008) Phytochemistry , vol.69 , pp. 2449-2456
    • Silber, M.V.1    Meimberg, H.2    Ebel, J.3
  • 34
    • 84872497791 scopus 로고    scopus 로고
    • Analysis of five rice 4-coumarate:Coenzyme A ligase enzyme activity and stress response for potential roles in lignin and flavonoid biosynthesis in rice
    • Sun, H.; Li, Y.; Feng, S.; Zou, W.; Guo, K.; Fan, C.; Si, S.; Peng, L. Analysis of five rice 4-coumarate:coenzyme A ligase enzyme activity and stress response for potential roles in lignin and flavonoid biosynthesis in rice. Biochem. Biophys. Res. Commun. 2013, 430, 1151-1156.
    • (2013) Biochem. Biophys. Res. Commun , vol.430 , pp. 1151-1156
    • Sun, H.1    Li, Y.2    Feng, S.3    Zou, W.4    Guo, K.5    Fan, C.6    Si, S.7    Peng, L.8
  • 36
    • 77953053139 scopus 로고    scopus 로고
    • Structure and function of the chalcone synthase superfamily of plant type III polyketide synthases
    • Abe, I.; Morita, H. Structure and function of the chalcone synthase superfamily of plant type III polyketide synthases. Nat. Prod. Rep. 2010, 27, 809-838.
    • (2010) Nat. Prod. Rep , vol.27 , pp. 809-838
    • Abe, I.1    Morita, H.2
  • 37
    • 80455164748 scopus 로고    scopus 로고
    • Chalcone synthase and its functions in plant resistance
    • Dao, T.T.H.; Linthorst, H.J.M.; Verpoorte, R. Chalcone synthase and its functions in plant resistance. Phytochem. Rev. 2011, 10, 397-412.
    • (2011) Phytochem. Rev , vol.10 , pp. 397-412
    • Dao, T.T.H.1    Linthorst, H.J.M.2    Verpoorte, R.3
  • 38
    • 57749175935 scopus 로고    scopus 로고
    • PKS activities and biosynthesis of cannabinoids and flavonoids in Cannabis sativa L. plants
    • Flores-Sanchez, I.J.; Verpoorte, R. PKS activities and biosynthesis of cannabinoids and flavonoids in Cannabis sativa L. plants. Plant Cell Physiol. 2008, 49, 1767-1782.
    • (2008) Plant Cell Physiol , vol.49 , pp. 1767-1782
    • Flores-Sanchez, I.J.1    Verpoorte, R.2
  • 39
    • 0028155769 scopus 로고
    • The flavonoid biosynthetic pathway in plants: Function and evolution
    • Koes, R.E.; Quattrocchio, F.; Mol, J.N.M. The flavonoid biosynthetic pathway in plants: Function and evolution. BioEssays 1994, 16, 123-132.
    • (1994) BioEssays , vol.16 , pp. 123-132
    • Koes, R.E.1    Quattrocchio, F.2    Mol, J.N.M.3
  • 40
    • 37549048671 scopus 로고    scopus 로고
    • Differential expression of genes involved in C1 metabolism and lignin biosynthesis in wooden core and bast tissues of fibre hemp (Cannabis sativa L.)
    • Van den Broeck, H.C.; Maliepaard, C.; Ebskamp, M.J.M.; Toonen, M.A.J.; Koops, A.J. Differential expression of genes involved in C1 metabolism and lignin biosynthesis in wooden core and bast tissues of fibre hemp (Cannabis sativa L.). Plant Sci. 2008, 174, 205-220.
    • (2008) Plant Sci , vol.174 , pp. 205-220
    • Van den Broeck, H.C.1    Maliepaard, C.2    Ebskamp, M.J.M.3    Toonen, M.A.J.4    Koops, A.J.5
  • 41
    • 0024988375 scopus 로고
    • Protein database searches for multiple alignments
    • Altschul, S.F.; Lipman, D.J. Protein database searches for multiple alignments. Proc. Natl. Acad. Sci. USA 1990, 87, 5509-5513.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5509-5513
    • Altschul, S.F.1    Lipman, D.J.2
  • 42
    • 84879903335 scopus 로고    scopus 로고
    • Available online, accessed on 12 February
    • SIB Swiss institute of Bioinformatic Home page. Available online: http://www.expasy.ch/tools/scanprosite (accessed on 12 February 2013).
    • (2013) SIB Swiss Institute of Bioinformatic Home Page
  • 43
    • 84894896207 scopus 로고    scopus 로고
    • Discovery and role of methylidene imidazolone, a highly electrophylic prosthetic group
    • Rétey, J. Discovery and role of methylidene imidazolone, a highly electrophylic prosthetic group. Biochem. Biophys. Acta 2003, 424, 233-242.
    • (2003) Biochem. Biophys. Acta , vol.424 , pp. 233-242
    • Rétey, J.1
  • 44
    • 34347376588 scopus 로고    scopus 로고
    • A modern view of phenylalanine ammonia-lyase
    • MacDonald, M.J.; D'Cunha, G.B. A modern view of phenylalanine ammonia-lyase. Biochem. Cell Biol. 2007, 85, 273-282.
    • (2007) Biochem. Cell Biol , vol.85 , pp. 273-282
    • Macdonald, M.J.1    D'cunha, G.B.2
  • 45
    • 0032811334 scopus 로고    scopus 로고
    • Phosphorylation of phenylalanine ammonia-lyase: Evidence for a novel protein kinase and identification of the phosphorylated residue
    • Allwood, E.G.; Davies, D.R.; Gerrish, C.; Ellis, B.E.; Bolwell, G.P. Phosphorylation of phenylalanine ammonia-lyase: Evidence for a novel protein kinase and identification of the phosphorylated residue. FEBS Lett. 1999, 457, 47-52.
    • (1999) FEBS Lett , vol.457 , pp. 47-52
    • Allwood, E.G.1    Davies, D.R.2    Gerrish, C.3    Ellis, B.E.4    Bolwell, G.P.5
  • 46
    • 13444301492 scopus 로고    scopus 로고
    • Molecular phenotyping of the pal1 and pal2 mutants of Arabidopsis thaliana reveals far-reaching consequences on phenylpropanoid, amino Acid, and carbohydrate metabolism
    • Rohde, A.; Morreel, K.; Ralph, J.; Goeminne, G.; Hostyn, V.; de Rycke, R.; Kushnir, S.; van Doorsselaere, J.; Joseleau, J.P.; Vuylsteke, M.; et al. Molecular phenotyping of the pal1 and pal2 mutants of Arabidopsis thaliana reveals far-reaching consequences on phenylpropanoid, amino Acid, and carbohydrate metabolism. Plant Cell 2004, 16, 2749-2771.
    • (2004) Plant Cell , vol.16 , pp. 2749-2771
    • Rohde, A.1    Morreel, K.2    Ralph, J.3    Goeminne, G.4    Hostyn, V.5    de Rycke, R.6    Kushnir, S.7    van Doorsselaere, J.8    Joseleau, J.P.9    Vuylsteke, M.10
  • 47
    • 77955666376 scopus 로고    scopus 로고
    • Functional analysis of the arabidopsis PAL gene family in plant growth, development, and response to environmental stress
    • Huang, J.L.; Gu, M.; Lai, Z.B.; Fan, B.F.; Shi, K.; Zhou, Y.H.; Yu, J.Q.; Chen, Z.X. Functional analysis of the arabidopsis PAL gene family in plant growth, development, and response to environmental stress. Plant Physiol. 2010, 153, 1526-1538.
    • (2010) Plant Physiol , vol.153 , pp. 1526-1538
    • Huang, J.L.1    Gu, M.2    Lai, Z.B.3    Fan, B.F.4    Shi, K.5    Zhou, Y.H.6    Yu, J.Q.7    Chen, Z.X.8
  • 48
    • 84856221647 scopus 로고    scopus 로고
    • The PAL2 promoter activities in relation to structural development and adaptation in Arabidopsis thaliana
    • Wong, J.H.; Namasivayam, P.; Abdullah, M.P. The PAL2 promoter activities in relation to structural development and adaptation in Arabidopsis thaliana. Planta 2012, 235, 267-277.
    • (2012) Planta , vol.235 , pp. 267-277
    • Wong, J.H.1    Namasivayam, P.2    Abdullah, M.P.3
  • 50
    • 0035920183 scopus 로고    scopus 로고
    • Identification of the substrate specificity-conferring amino acid residues of 4-coumarate:CoenzymeA ligase allows the rational design of mutant enzymes with new catalytic properties
    • Stuible, H.P.; Kombrink, E. Identification of the substrate specificity-conferring amino acid residues of 4-coumarate:coenzymeA ligase allows the rational design of mutant enzymes with new catalytic properties. J. Biol. Chem. 2001, 276, 26893-26897.
    • (2001) J. Biol. Chem , vol.276 , pp. 26893-26897
    • Stuible, H.P.1    Kombrink, E.2
  • 51
    • 0036187913 scopus 로고    scopus 로고
    • Extensive feature detection of N-terminal protein sorting signals
    • Bannai, H.; Tamada, Y.; Maruyama, O.; Nakai, K.; Miyano, S. Extensive feature detection of N-terminal protein sorting signals. Bioinformatics 2002, 18, 298-305.
    • (2002) Bioinformatics , vol.18 , pp. 298-305
    • Bannai, H.1    Tamada, Y.2    Maruyama, O.3    Nakai, K.4    Miyano, S.5
  • 52
    • 80053581937 scopus 로고    scopus 로고
    • Functional characterization of evolutionarily divergent 4-coumarate:Coenzyme A ligases in rice
    • Gui, J.; Shen, J.; Li, L. Functional characterization of evolutionarily divergent 4-coumarate:coenzyme A ligases in rice. Plant Physiol. 2011, 157, 574-586.
    • (2011) Plant Physiol , vol.157 , pp. 574-586
    • Gui, J.1    Shen, J.2    Li, L.3
  • 53
    • 0029140785 scopus 로고
    • The phenylalanine ammonia-lyase gene family in Arabidopsis thaliana
    • Wanner, L.A.; Li, G.; Ware, D.; Somssich, I.E.; Davis, K.R. The phenylalanine ammonia-lyase gene family in Arabidopsis thaliana. Plant Mol. Biol. 1995, 27, 327-338.
    • (1995) Plant Mol. Biol , vol.27 , pp. 327-338
    • Wanner, L.A.1    Li, G.2    Ware, D.3    Somssich, I.E.4    Davis, K.R.5
  • 54
    • 0026637937 scopus 로고
    • Truncated phenylalanine ammonia-lyase expression in tomato (Lycopersicon esculentum)
    • Lee, S.W.; Robb, J.; Nazar, R.N. Truncated phenylalanine ammonia-lyase expression in tomato (Lycopersicon esculentum). J. Biol. Chem. 1992, 267, 11824-11830.
    • (1992) J. Biol. Chem , vol.267 , pp. 11824-11830
    • Lee, S.W.1    Robb, J.2    Nazar, R.N.3
  • 55
    • 0039552100 scopus 로고    scopus 로고
    • Three 4-coumarate: Coenzyme A ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms
    • Ehlting, J.; Buttner, D.; Wang, Q.; Douglas, C.J.; Somssich, I.E.; Kombrink, E. Three 4-coumarate: Coenzyme A ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms. Plant J. 1999, 19, 9-20.
    • (1999) Plant J , vol.19 , pp. 9-20
    • Ehlting, J.1    Buttner, D.2    Wang, Q.3    Douglas, C.J.4    Somssich, I.E.5    Kombrink, E.6
  • 56
    • 1942517801 scopus 로고    scopus 로고
    • Evolution of 4-coumarate: Cenzyme A ligase (4CL) gene and divergence of Larix. (Pinaceae)
    • Wei, X.X.; Wang, X.-Q. Evolution of 4-coumarate: Cenzyme A ligase (4CL) gene and divergence of Larix. (Pinaceae). Mol. Physiogen. Evol. 2004, 31, 542-553.
    • (2004) Mol. Physiogen. Evol , vol.31 , pp. 542-553
    • Wei, X.X.1    Wang, X.-Q.2
  • 57
    • 3242798222 scopus 로고
    • Phenylalanine and tyrosine ammonia-lyase activity in Sporobolomyces pararoseus
    • Parkhurst, J.R.; Hodgins, B.S. Phenylalanine and tyrosine ammonia-lyase activity in Sporobolomyces pararoseus. Phytochemistry 1971, 10, 2997-3000.
    • (1971) Phytochemistry , vol.10 , pp. 2997-3000
    • Parkhurst, J.R.1    Hodgins, B.S.2
  • 58
    • 1842287997 scopus 로고    scopus 로고
    • Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity
    • Rösler, J.; Krekel, F.; Amrhein, N.; Schmid, J. Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity. Plant Physiol. 1997, 113, 175-179.
    • (1997) Plant Physiol , vol.113 , pp. 175-179
    • Rösler, J.1    Krekel, F.2    Amrhein, N.3    Schmid, J.4
  • 59
    • 78249234153 scopus 로고    scopus 로고
    • Cloning, expression, site-directed mutagenesis and immunolocalization of phenylalanine ammonia-lyase in Bambusa oldhamii
    • Hsieh, L.-S.; Ma, G.-J.; Yang, C.-C.; Lee, P.-D. Cloning, expression, site-directed mutagenesis and immunolocalization of phenylalanine ammonia-lyase in Bambusa oldhamii. Phytochemistry 2010, 71, 1999-2009.
    • (2010) Phytochemistry , vol.71 , pp. 1999-2009
    • Hsieh, L.-S.1    Ma, G.-J.2    Yang, C.-C.3    Lee, P.-D.4
  • 60
    • 0026537109 scopus 로고
    • Identification by high-performance liquid chromatography of tyrosine ammonia-lyase activity in purified fractions of Phaseulus vulgaris phenylalanine ammonia-lyase
    • Scott, D.A.; Hammond, P.M.; Brearley, G.M.; Price, C.P. Identification by high-performance liquid chromatography of tyrosine ammonia-lyase activity in purified fractions of Phaseulus vulgaris phenylalanine ammonia-lyase. J. Chromatogr. 1992, 573, 309-312.
    • (1992) J. Chromatogr , vol.573 , pp. 309-312
    • Scott, D.A.1    Hammond, P.M.2    Brearley, G.M.3    Price, C.P.4
  • 61
    • 84863027089 scopus 로고    scopus 로고
    • Fungal and plant phenylalanine ammonia-lyase
    • Hyun, M.W.; Yun, Y.H.; Kim, J.Y.; Kim, S.H. Fungal and plant phenylalanine ammonia-lyase. Mycobiology 2011, 39, 257-265.
    • (2011) Mycobiology , vol.39 , pp. 257-265
    • Hyun, M.W.1    Yun, Y.H.2    Kim, J.Y.3    Kim, S.H.4
  • 62
    • 44649173032 scopus 로고    scopus 로고
    • Unusually divergent 4-coumarate:CoA-ligases from Ruta graveolens L
    • Endler, A.; Martens, S.; Wellmann, F.; Matern, U. Unusually divergent 4-coumarate:CoA-ligases from Ruta graveolens L. Plant Mol. Biol. 2008, 67, 335-346.
    • (2008) Plant Mol. Biol , vol.67 , pp. 335-346
    • Endler, A.1    Martens, S.2    Wellmann, F.3    Matern, U.4
  • 63
    • 77749320523 scopus 로고    scopus 로고
    • NMR-based metabolomic analysis of plants
    • Kim, K.H.; Choi, Y.H.; Verpoorte, R. NMR-based metabolomic analysis of plants. Nat. Prot. 2010, 5, 536-549.
    • (2010) Nat. Prot , vol.5 , pp. 536-549
    • Kim, K.H.1    Choi, Y.H.2    Verpoorte, R.3
  • 64
    • 84879962591 scopus 로고    scopus 로고
    • version 1.3, software for NMR data acquisition and processing. Bruker BioSpin GmbH: Rheistetten, Germany
    • Topsin Bruker, version 1.3, software for NMR data acquisition and processing. Bruker BioSpin GmbH: Rheistetten, Germany, 2003.
    • (2003)
    • Bruker, T.1
  • 65
    • 84879528002 scopus 로고    scopus 로고
    • PrimmBiotech, Inc, Available online, accessed on 25 January
    • PrimmBiotech, Inc. Home page. Available online: http://www.primmbiotech.com (accessed on 25 January 2013).
    • (2013) Home Page
  • 66
    • 84879932830 scopus 로고    scopus 로고
    • Blastx basic local alignment search tool Home page. Available online, accessed on 10 February
    • Blastx basic local alignment search tool Home page. Available online: http://blast.ncbi.nlm.nih.gov (accessed on 10 February 2013).
    • (2013)
  • 67
    • 84879906128 scopus 로고    scopus 로고
    • CLUSTALW. Available online, accessed on 4 March
    • CLUSTALW. Available online: http://align.genome.jp/ (accessed on 4 March 2013).
    • (2013)
  • 68
    • 0028829961 scopus 로고
    • Stress-induced phenylpropanoid metabolism
    • Dixon, R.A.; Paiva, N.L. Stress-induced phenylpropanoid metabolism. Plant Cell 1995, 7, 1085-1097.
    • (1995) Plant Cell , vol.7 , pp. 1085-1097
    • Dixon, R.A.1    Paiva, N.L.2
  • 69
    • 0023375195 scopus 로고
    • The neighbor-joining method-A new method for reconstructing phylogenetic trees
    • Saitou, N.; Nei, M. The neighbor-joining method-A new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 1987, 4, 406-425.
    • (1987) Mol. Biol. Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 70
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall, T.A. BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp. Ser. 1999, 41, 95-98.
    • (1999) Nucleic Acids Symp. Ser , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 71
    • 84879968036 scopus 로고    scopus 로고
    • Primer3, version 0.4.0, software for primers design. Whitehead Institute for Biomedical Research: Cambridge, MA, USA
    • Primer3, version 0.4.0, software for primers design. Whitehead Institute for Biomedical Research: Cambridge, MA, USA, 2007.
    • (2007)
  • 72
    • 84879923147 scopus 로고    scopus 로고
    • Primer 3 Home page. Available online, accessed on 13 November
    • Primer 3 Home page. Available online: http://primer3.wi.mit.edu (accessed on 13 November 2012).
    • (2012)
  • 73
    • 84879940647 scopus 로고    scopus 로고
    • Premier biosoft Home page. Available online, accessed on 20 February
    • Premier biosoft Home page. Available online: http://www.premierbiosoft.com/molecular_beacons/index.html (accessed on 20 February 2013).
    • (2013)
  • 74
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura, K.; Peterson, D.; Peterson, N.; Stecher, G.; Nei, M.; Kumar, S. MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol. Biol. Evol. 2011, 28, 2731-2739.
    • (2011) Mol. Biol. Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 75
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time PCR
    • Pfaffl, M.W. A new mathematical model for relative quantification in real-time PCR. Nucl. Acids Res. 2001, 29, 2002-2007.
    • (2001) Nucl. Acids Res , vol.29 , pp. 2002-2007
    • Pfaffl, M.W.1
  • 76
    • 77954535498 scopus 로고    scopus 로고
    • Enzyme of phenylpropanoid metabolism in the important medicinal plant Melissa officinalis L
    • Weitzel, C.; Petersen, M. Enzyme of phenylpropanoid metabolism in the important medicinal plant Melissa officinalis L. Planta 2010, 232, 731-742.
    • (2010) Planta , vol.232 , pp. 731-742
    • Weitzel, C.1    Petersen, M.2
  • 77
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 78
    • 0041113470 scopus 로고
    • Phytochrome controlled phenylalanine ammonia lyase activity in Hordeum vulgare plastids
    • Saunders, J.A.; McClure, J.W. Phytochrome controlled phenylalanine ammonia lyase activity in Hordeum vulgare plastids. Phytochemistry 1975, 14, 1285-1289.
    • (1975) Phytochemistry , vol.14 , pp. 1285-1289
    • Saunders, J.A.1    McClure, J.W.2
  • 79
    • 29944445042 scopus 로고    scopus 로고
    • Changes and subcellular localizations of the enzymes involved in phenylpropanoid metabolism during grape berry development
    • Chen, J.-Y.; Wen, P.-F; Kong, W.-F.; Pan, Q.-H.; Wan, S.-B.; Huang, W.-D. Changes and subcellular localizations of the enzymes involved in phenylpropanoid metabolism during grape berry development. J. Plant Physiol. 2006, 163, 115-127.
    • (2006) J. Plant Physiol , vol.163 , pp. 115-127
    • Chen, J.-Y.1    Wen P.-F2    Kong, W.-F.3    Pan, Q.-H.4    Wan, S.-B.5    Huang, W.-D.6
  • 80
    • 0036960021 scopus 로고    scopus 로고
    • Comparison of different methods for lignin determination as a basis for calibration of near-infrared reflectance spectroscopy and implications of lignoproteins
    • Brinkmann, K.; Blaschke, L.; Polle, A. Comparison of different methods for lignin determination as a basis for calibration of near-infrared reflectance spectroscopy and implications of lignoproteins. J. Chem. Ecol. 2002, 28, 2483-2501.
    • (2002) J. Chem. Ecol , vol.28 , pp. 2483-2501
    • Brinkmann, K.1    Blaschke, L.2    Polle, A.3


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