메뉴 건너뛰기




Volumn 109, Issue 40, 2012, Pages 16383-16388

Completion of the core β-oxidative pathway of benzoic acid biosynthesis in plants

Author keywords

Benzenoid network; Floral scent; Multifunctional protein

Indexed keywords

AROMATIC COMPOUND; BENZOIC ACID; CINNAMIC ACID; CINNAMOYL COENZYME A HYDRATASE DEHYDROGENASE; COENZYME A; PHENYLALANINE; UNCLASSIFIED DRUG;

EID: 84867039055     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1211001109     Document Type: Article
Times cited : (147)

References (47)
  • 2
    • 85056685255 scopus 로고    scopus 로고
    • (CRC, Boca Raton, FL), 3rd Ed
    • Chipley J (2005) Antimicrobials in Food (CRC, Boca Raton, FL), 3rd Ed, pp 11-48.
    • (2005) Antimicrobials in Food , pp. 11-48
    • Chipley, J.1
  • 3
    • 0344161262 scopus 로고    scopus 로고
    • + currents by benzocaine homologs
    • Quan C, Mok WM, Wang GK (1996) Use-dependent inhibition of Na+ currents by benzocaine homologs. Biophys J 70:194-201. (Pubitemid 26021460)
    • (1996) Biophysical Journal , vol.70 , Issue.1 , pp. 194-201
    • Quan, C.1    Mok, W.M.2    Wang, G.K.3
  • 4
    • 77955391041 scopus 로고    scopus 로고
    • Studies of the essential oil composition, antibacterial and antifungal activity profiles of Frankenia laevis L. from Tunisia
    • Saïdana D, et al. (2010) Studies of the essential oil composition, antibacterial and antifungal activity profiles of Frankenia laevis L. from Tunisia. J Essent Oil Res 22: 349-353.
    • (2010) J Essent Oil Res , vol.22 , pp. 349-353
    • Saïdana, D.1
  • 5
    • 0344984320 scopus 로고    scopus 로고
    • Production of Taxol and its Analogues from Cell Cultures of Taxus wallichiana
    • DOI 10.1076/phbi.41.6.426.17822
    • Veeresham C, Mamatha R, Babu CP, Srisilam K, Kokate CK (2003) Production of taxol and its analogues from cell cultures of Taxus wallichiana. Pharm Biol 41:426-430. (Pubitemid 37468121)
    • (2003) Pharmaceutical Biology , vol.41 , Issue.6 , pp. 426-430
    • Veeresham, C.1    Mamatha, R.2    Prasad, B.C..3    Srisilam, K.4    Kokate, C.K.5
  • 6
    • 0027132224 scopus 로고
    • Pathway of salicylic acid biosynthesis in healthy and virus-inoculated tobacco
    • Yalpani N, Leon J, Lawton MA, Raskin I (1993) Pathway of salicylic acid biosynthesis in healthy and virus-inoculated tobacco. Plant Physiol 103:315-321. (Pubitemid 2005196)
    • (1993) Plant Physiology , vol.103 , Issue.2 , pp. 315-321
    • Yalpani, N.1    Leon, J.2    Lawton, M.A.3    Raskin, I.4
  • 7
    • 0028796938 scopus 로고
    • Salicylic acid in rice: Biosynthesis, conjugation, and possible role
    • Silverman P, et al. (1995) Salicylic acid in rice: Biosynthesis, conjugation, and possible role. Plant Physiol 108:633-639.
    • (1995) Plant Physiol , vol.108 , pp. 633-639
    • Silverman, P.1
  • 8
    • 0001140063 scopus 로고    scopus 로고
    • The biosynthesis of salicylic acid in potato plants
    • Coquoz JL, Buchala A, Metraux JP (1998) The biosynthesis of salicylic acid in potato plants. Plant Physiol 117:1095-1101. (Pubitemid 128652882)
    • (1998) Plant Physiology , vol.117 , Issue.3 , pp. 1095-1101
    • Coquoz, J.-L.1    Buchala, A.2    Metraux, J.-P.3
  • 9
    • 0034480179 scopus 로고    scopus 로고
    • 3-hydroxy-3-phenylpropanoic acid is an intermediate in the biosynthesis of benzoic acid and salicylic acid but benzaldehyde is not
    • DOI 10.1007/s004250000377
    • Jarvis AP, Schaaf O, Oldham NJ (2000) 3-hydroxy-3-phenylpropanoic acid is an intermediate in the biosynthesis of benzoic acid and salicylic acid but benzaldehyde is not. Planta 212:119-126. (Pubitemid 32139903)
    • (2000) Planta , vol.212 , Issue.1 , pp. 119-126
    • Jarvis, A.P.1    Schaaf, O.2    Oldham, N.J.3
  • 10
    • 0035496654 scopus 로고    scopus 로고
    • A mechanism of benzoic acid biosynthesis in plants and bacteria that mirrors fatty acid beta-oxidation
    • Hertweck C, Jarvis AP, Xiang L, Moore BS, Oldham NJ (2001) A mechanism of benzoic acid biosynthesis in plants and bacteria that mirrors fatty acid beta-oxidation. ChemBioChem 2:784-786. (Pubitemid 33722635)
    • (2001) ChemBioChem , vol.2 , Issue.10 , pp. 784-786
    • Hertweck, C.1    Jarvis, A.P.2    Xiang, L.3    Moore, B.S.4    Oldham, N.J.5
  • 11
    • 0036934797 scopus 로고    scopus 로고
    • Benzoic acid biosynthesis in cell cultures of Hypericum androsaemum
    • Abd El-Mawla AM, Beerhues L (2002) Benzoic acid biosynthesis in cell cultures of Hypericum androsaemum. Planta 214:727-733.
    • (2002) Planta , vol.214 , pp. 727-733
    • Abd El-Mawla, A.M.1    Beerhues, L.2
  • 12
    • 67649718423 scopus 로고    scopus 로고
    • Involvement of snapdragon benzaldehyde dehydrogenase in benzoic acid biosynthesis
    • Long MC, et al. (2009) Involvement of snapdragon benzaldehyde dehydrogenase in benzoic acid biosynthesis. Plant J 59:256-265.
    • (2009) Plant J , vol.59 , pp. 256-265
    • Long, M.C.1
  • 15
    • 0037092062 scopus 로고    scopus 로고
    • Purification and characterization of benzoate:coenzyme A ligase from Clarkia breweri
    • DOI 10.1016/S0003-9861(02)00026-7, PII S0003986102000267
    • Beuerle T, Pichersky E (2002) Purification and characterization of benzoate:coenzyme A ligase from Clarkia breweri. Arch Biochem Biophys 400:258-264. (Pubitemid 34852406)
    • (2002) Archives of Biochemistry and Biophysics , vol.400 , Issue.2 , pp. 258-264
    • Beuerle, T.1    Pichersky, E.2
  • 16
    • 33646121742 scopus 로고    scopus 로고
    • Variations on a theme: Synthesis and modification of plant benzoic acids
    • Wildermuth MC (2006) Variations on a theme: Synthesis and modification of plant benzoic acids. Curr Opin Plant Biol 9:288-296.
    • (2006) Curr Opin Plant Biol , vol.9 , pp. 288-296
    • Wildermuth, M.C.1
  • 17
    • 84863105916 scopus 로고    scopus 로고
    • Contribution of CoA ligases to benzenoid biosynthesis in petunia flowers
    • Klempien A, et al. (2012) Contribution of CoA ligases to benzenoid biosynthesis in petunia flowers. Plant Cell 24:2015-2030.
    • (2012) Plant Cell , vol.24 , pp. 2015-2030
    • Klempien, A.1
  • 18
  • 19
    • 44949151664 scopus 로고    scopus 로고
    • Seed storage oil mobilization
    • Graham IA (2008) Seed storage oil mobilization. Annu Rev Plant Biol 59:115- 142.
    • (2008) Annu Rev Plant Biol , vol.59 , pp. 115-142
    • Graham, I.A.1
  • 21
    • 0033212993 scopus 로고    scopus 로고
    • A defect in β-oxidation causes abnormal inflorescence development in Arabidopsis
    • Richmond TA, Bleecker AB (1999) A defect in β-oxidation causes abnormal inflorescence development in Arabidopsis. Plant Cell 11:911-1923.
    • (1999) Plant Cell , vol.11 , pp. 911-1923
    • Richmond, T.A.1    Bleecker, A.B.2
  • 22
    • 33644786913 scopus 로고    scopus 로고
    • The Arabidopsis thaliana multifunctional protein gene (MFP2) of peroxisomal β-oxidation is essential for seedling establishment
    • DOI 10.1111/j.1365-313X.2005.02650.x
    • Rylott EL, et al. (2006) The Arabidopsis thaliana multifunctional protein gene (MFP2) of peroxisomal β-oxidation is essential for seedling establishment. Plant J 45:930-941. (Pubitemid 43344755)
    • (2006) Plant Journal , vol.45 , Issue.6 , pp. 930-941
    • Rylott, E.L.1    Eastmond, P.J.2    Gilday, A.D.3    Slocombe, S.P.4    Larson, T.R.5    Baker, A.6    Graham, I.A.7
  • 23
    • 77953225602 scopus 로고    scopus 로고
    • RNAi suppression of Arogenate Dehydratase1 reveals that phenylalanine is synthesized predominantly via the arogenate pathway in petunia petals
    • Maeda H, et al. (2010) RNAi suppression of Arogenate Dehydratase1 reveals that phenylalanine is synthesized predominantly via the arogenate pathway in petunia petals. Plant Cell 22:832-849.
    • (2010) Plant Cell , vol.22 , pp. 832-849
    • Maeda, H.1
  • 24
    • 0037169490 scopus 로고    scopus 로고
    • Identification of a rice RNA- and microtubule-binding protein as the multifunctional protein, a peroxisomal enzyme involved in the beta-oxidation of fatty acids
    • DOI 10.1074/jbc.M109510200
    • Chuong SDX, Mullen RT, Muench DG (2002) Identification of a rice RNA- and microtubule-binding protein as the multifunctional protein, a peroxisomal enzyme involved in the beta -oxidation of fatty acids. J Biol Chem 277:2419-2429. (Pubitemid 34953263)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.4 , pp. 2419-2429
    • Chuong, S.D.X.1    Mullen, R.T.2    Muench, D.G.3
  • 25
    • 56449110279 scopus 로고    scopus 로고
    • A stress-responsive multifunctional protein involved in beta-oxidation in tobacco plants
    • Ohya H, Ogata A, Nakamura K, Chung K, Sano H (2008) A stress-responsive multifunctional protein involved in beta-oxidation in tobacco plants. Plant Biotechnol 25: 503-508.
    • (2008) Plant Biotechnol , vol.25 , pp. 503-508
    • Ohya, H.1    Ogata, A.2    Nakamura, K.3    Chung, K.4    Sano, H.5
  • 26
    • 0028102553 scopus 로고
    • Domains of the tetrafunctional protein acting in glyoxysomal fatty acid beta-oxidation. Demonstration of epimerase and isomerase activities on a peptide lacking hydratase activity
    • Preisig-Müller R, Gühnemann-Schäfer K, Kindl H (1994) Domains of the tetrafunctional protein acting in glyoxysomal fatty acid beta-oxidation. Demonstration of epimerase and isomerase activities on a peptide lacking hydratase activity. J Biol Chem 269:20475-20481.
    • (1994) J Biol Chem , vol.269 , pp. 20475-20481
    • Preisig-Müller, R.1    Gühnemann-Schäfer, K.2    Kindl, H.3
  • 27
    • 16544384619 scopus 로고    scopus 로고
    • AraPerox. A database of putative arabidopsis proteins from plant peroxisomes
    • DOI 10.1104/pp.104.043695
    • Reumann S, Ma C, Lemke S, Babujee L (2004) AraPerox. A database of putative Arabidopsis proteins from plant peroxisomes. Plant Physiol 136:2587-2608. (Pubitemid 41071300)
    • (2004) Plant Physiology , vol.136 , Issue.1 , pp. 2587-2608
    • Reumann, S.1    Ma, C.2    Lemke, S.3    Babujee, L.4
  • 28
    • 0026674967 scopus 로고
    • Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase
    • Nichols BP, Green JM (1992) Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase. J Bacteriol 174:5309-5316.
    • (1992) J Bacteriol , vol.174 , pp. 5309-5316
    • Nichols, B.P.1    Green, J.M.2
  • 29
    • 0037077213 scopus 로고    scopus 로고
    • Salicylate biosynthesis in Pseudomonas aeruginosa. Purification and characterization of PchB, a novel bifunctional enzyme displaying isochorismate pyruvate-lyase and chorismate mutase activities
    • DOI 10.1074/jbc.M202410200
    • Gaille C, Kast P, Haas D (2002) Salicylate biosynthesis in Pseudomonas aeruginosa. Purification and characterization of PchB, a novel bifunctional enzyme displaying isochorismate pyruvate-lyase and chorismate mutase activities. J Biol Chem 277: 21768-21775. (Pubitemid 34952328)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.24 , pp. 21768-21775
    • Gaille, C.1    Kast, P.2    Dieter, H.3
  • 30
    • 0001603268 scopus 로고
    • Biosynthesis of the benzoyl moiety of cocaine from cinnamic acid via (R)-(+)-3-hydroxy-3-phenylpropanoic acid
    • Bjorklund JA, Leete E (1992) Biosynthesis of the benzoyl moiety of cocaine from cinnamic acid via (R)-(+)-3-hydroxy-3-phenylpropanoic acid. Phytochemistry 31: 3883-3887.
    • (1992) Phytochemistry , vol.31 , pp. 3883-3887
    • Bjorklund, J.A.1    Leete, E.2
  • 31
    • 0033815884 scopus 로고    scopus 로고
    • New advances in coenzyme Q biosynthesis
    • Clarke CF (2000) New advances in coenzyme Q biosynthesis. Protoplasma 213: 134-147.
    • (2000) Protoplasma , vol.213 , pp. 134-147
    • Clarke, C.F.1
  • 32
    • 0036138649 scopus 로고    scopus 로고
    • Pathways of straight and branched chain fatty acid catabolism in higher plants
    • DOI 10.1016/S0163-7827(01)00022-4, PII S0163782701000224
    • Graham IA, Eastmond PJ (2002) Pathways of straight and branched chain fatty acid catabolism in higher plants. Prog Lipid Res 41:156-181. (Pubitemid 34037869)
    • (2002) Progress in Lipid Research , vol.41 , Issue.2 , pp. 156-181
    • Graham, I.A.1    Eastmond, P.J.2
  • 33
    • 0036154857 scopus 로고    scopus 로고
    • Control of mitochondrial β-oxidation flux
    • Eaton S (2002) Control of mitochondrial β-oxidation flux. Prog Lipid Res 41:197-239.
    • (2002) Prog Lipid Res , vol.41 , pp. 197-239
    • Eaton, S.1
  • 36
    • 0030662714 scopus 로고    scopus 로고
    • Transport of activated fatty acids by the peroxisomal ATP-binding-cassette transporter Pxa2 in a semi-intact yeast cell system
    • Verleur N, Hettema EH, van Roermund CWT, Tabak HF, Wanders RJA (1997) Transport of activated fatty acids by the peroxisomal ATP-binding-cassette transporter Pxa2 in a semi-intact yeast cell system. Eur J Biochem 249:657-661. (Pubitemid 27479034)
    • (1997) European Journal of Biochemistry , vol.249 , Issue.3 , pp. 657-661
    • Verleur, N.1    Hettema, E.H.2    Van Roermund, C.W.T.3    Tabak, H.F.4    Wanders, R.J.A.5
  • 37
    • 77956922124 scopus 로고    scopus 로고
    • The Arabidopsis peroxisomal ABC transporter, comatose, complements the Saccharomyces cerevisiae pxa1 pxa2Δ mutant for metabolism of long-chain fatty acids and exhibits fatty acyl-CoA-stimulated ATPase activity
    • Nyathi Y, et al. (2010) The Arabidopsis peroxisomal ABC transporter, comatose, complements the Saccharomyces cerevisiae pxa1 pxa2Δ mutant for metabolism of long-chain fatty acids and exhibits fatty acyl-CoA-stimulated ATPase activity. J Biol Chem 285:29892-29902.
    • (2010) J Biol Chem , vol.285 , pp. 29892-29902
    • Nyathi, Y.1
  • 38
    • 84861875087 scopus 로고    scopus 로고
    • The acyl-acyl carrier protein synthetase from Synechocystis sp. PCC 6803 mediates fatty acid import
    • von Berlepsch S, et al. (2012) The acyl-acyl carrier protein synthetase from Synechocystis sp. PCC 6803 mediates fatty acid import. Plant Physiol 159:606-617.
    • (2012) Plant Physiol , vol.159 , pp. 606-617
    • Von Berlepsch, S.1
  • 39
    • 1942533552 scopus 로고    scopus 로고
    • On the Export of Fatty Acids from the Chloroplast
    • DOI 10.1074/jbc.M311305200
    • Koo AJK, Ohlrogge JB, Pollard M (2004) On the export of fatty acids from the chloroplast. J Biol Chem 279:16101-16110. (Pubitemid 38509301)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.16 , pp. 16101-16110
    • Koo, A.J.K.1    Ohlrogge, J.B.2    Pollard, M.3
  • 40
    • 84864409247 scopus 로고    scopus 로고
    • Phylloquinone (vitamin K(1)) biosynthesis in plants: Two peroxisomal thioesterases of lactobacillales origin hydrolyze 1,4-dihydroxy-2-naphthoyl- coa
    • Widhalm JR, et al. (2012) Phylloquinone (vitamin K(1)) biosynthesis in plants: two peroxisomal thioesterases of lactobacillales origin hydrolyze 1,4-dihydroxy-2-naphthoyl- coa. Plant J 71:205-215.
    • (2012) Plant J , vol.71 , pp. 205-215
    • Widhalm, J.R.1
  • 41
    • 53149085259 scopus 로고    scopus 로고
    • Novel functions of acyl-CoA thioesterases and acyltransferases as auxiliary enzymes in peroxisomal lipid metabolism
    • Hunt MC, Alexson SEH (2008) Novel functions of acyl-CoA thioesterases and acyltransferases as auxiliary enzymes in peroxisomal lipid metabolism. Prog Lipid Res 47: 405-421.
    • (2008) Prog Lipid Res , vol.47 , pp. 405-421
    • Hunt, M.C.1    Alexson, S.E.H.2
  • 42
    • 0037086137 scopus 로고    scopus 로고
    • Enzymatic synthesis and purification of aromatic coenzyme A esters
    • DOI 10.1006/abio.2001.5574
    • Beuerle T, Pichersky E (2002) Enzymatic synthesis and purification of aromatic coenzyme a esters. Anal Biochem 302:305-312. (Pubitemid 34229738)
    • (2002) Analytical Biochemistry , vol.302 , Issue.2 , pp. 305-312
    • Beuerle, T.1    Pichersky, E.2
  • 43
    • 0031879207 scopus 로고    scopus 로고
    • Acetoacetyl coenzyme a reductase and polyhydroxybutyrate synthesis in Rhizobium (Cicer) sp. strain CC 1192
    • Chohan SN, Copeland L (1998) Acetoacetyl coenzyme A reductase and polyhydroxybutyrate synthesis in rhizobium (Cicer) sp. Strain CC 1192. Appl Environ Microbiol 64:2859-2863. (Pubitemid 28363152)
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.8 , pp. 2859-2863
    • Chohan, S.N.1    Copeland, L.2
  • 44
    • 0033945137 scopus 로고    scopus 로고
    • Developmental regulation of methylbenzoate biosynthesis
    • Dudareva N, et al. (2000) Developmental regulation of methylbenzoate biosynthesis. Plant Cell 12:949-961.
    • (2000) Plant Cell , vol.12 , pp. 949-961
    • Dudareva, N.1
  • 45
    • 37049182668 scopus 로고
    • A simple and general method for transferring genes into plants
    • Horsch RB, et al. (1985) A simple and general method for transferring genes into plants. Science 227:1229-1231.
    • (1985) Science , vol.227 , pp. 1229-1231
    • Horsch, R.B.1
  • 46
    • 0028293431 scopus 로고
    • Recombinant liver fatty acid binding protein interacts with fatty acyl- coenzyme A
    • Hubbell T, Behnke WD, Woodford JK, Schroeder F (1994) Recombinant liver fatty acid binding protein interacts with fatty acyl-coenzyme A. Biochemistry 33:3327-3334. (Pubitemid 24112646)
    • (1994) Biochemistry , vol.33 , Issue.11 , pp. 3327-3334
    • Hubbell, T.1    Behnke, W.D.2    Woodford, J.K.3    Schroeder, F.4
  • 47
    • 81155137923 scopus 로고    scopus 로고
    • Profiling hydroxycinnamoyl-coenzyme A thioesters: Unlocking the back door of phenylpropanoid metabolism
    • Qualley AV, Cooper BR, Dudareva N (2012) Profiling hydroxycinnamoyl- coenzyme A thioesters: Unlocking the back door of phenylpropanoid metabolism. Anal Biochem 420:182-184.
    • (2012) Anal Biochem , vol.420 , pp. 182-184
    • Qualley, A.V.1    Cooper, B.R.2    Dudareva, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.