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Volumn 384, Issue 1, 2009, Pages 151-158

A cost-effective colorimetric assay for phenolic O-methyltransferases and characterization of caffeate 3-O-methyltransferases from Populus trichocarpa

Author keywords

Colorimetric assay; Gibbs' reagent; O Methyltransferase; Populus trichocarpa

Indexed keywords

AMINO ACIDS; COLOR; COLORIMETRY; COST EFFECTIVENESS; DISPLAY DEVICES; METHYLATION;

EID: 56249146987     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.09.031     Document Type: Article
Times cited : (6)

References (30)
  • 1
    • 0038374971 scopus 로고    scopus 로고
    • Many paths to methyltransfer: a chronicle of convergence
    • Schubert H.L., Blumenthal R.M., and Cheng X. Many paths to methyltransfer: a chronicle of convergence. Trends Biochem. Sci. 28 (2003) 329-335
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 329-335
    • Schubert, H.L.1    Blumenthal, R.M.2    Cheng, X.3
  • 2
    • 27844530636 scopus 로고    scopus 로고
    • Natural history of S-adenosylmethionine-binding proteins
    • Kozbial P.Z., and Mushegian A.R. Natural history of S-adenosylmethionine-binding proteins. BMC Struct. Biol. 5 (2005) 19
    • (2005) BMC Struct. Biol. , vol.5 , pp. 19
    • Kozbial, P.Z.1    Mushegian, A.R.2
  • 3
    • 77957028431 scopus 로고    scopus 로고
    • Structural, functional, and evolutionary basis for methylation of plant small molecules
    • Noel J.P., Dixon R.A., Pickersky E., Zubieta C., and Ferrer J.-L. Structural, functional, and evolutionary basis for methylation of plant small molecules. Rec. Adv. Phytochem. 37 (2003) 37-58
    • (2003) Rec. Adv. Phytochem. , vol.37 , pp. 37-58
    • Noel, J.P.1    Dixon, R.A.2    Pickersky, E.3    Zubieta, C.4    Ferrer, J.-L.5
  • 4
    • 0026495913 scopus 로고
    • Mammalian small molecule methyltransferase: their structural and functional features
    • Fujioka M. Mammalian small molecule methyltransferase: their structural and functional features. Int. J. Biochem. 24 (1992) 1917-1924
    • (1992) Int. J. Biochem. , vol.24 , pp. 1917-1924
    • Fujioka, M.1
  • 5
    • 0031882371 scopus 로고    scopus 로고
    • Plant O-methyltransferases: molecular analysis, common signature, and classification
    • Ibrahim R.K., Bruneau A., and Bantignies B. Plant O-methyltransferases: molecular analysis, common signature, and classification. Plant Mol. Biol. 36 (1998) 1-10
    • (1998) Plant Mol. Biol. , vol.36 , pp. 1-10
    • Ibrahim, R.K.1    Bruneau, A.2    Bantignies, B.3
  • 6
    • 0030814118 scopus 로고    scopus 로고
    • Identification of a phenolic 3-O-methyltransferase in the lignin-degrading fungus Phanerochaete chrysosporium
    • Jeffers M.R., McRoberts W.C., and Harper D.B. Identification of a phenolic 3-O-methyltransferase in the lignin-degrading fungus Phanerochaete chrysosporium. Microbiology 143 (1997) 1975-1981
    • (1997) Microbiology , vol.143 , pp. 1975-1981
    • Jeffers, M.R.1    McRoberts, W.C.2    Harper, D.B.3
  • 7
    • 1842817423 scopus 로고    scopus 로고
    • O-Methylation of benzaldehyde derivatives by "lignin specific" caffeic acid 3-O-methyltransferase
    • Kota P., Guo D., Zubieta C., Noel J., and Dixon R.A. O-Methylation of benzaldehyde derivatives by "lignin specific" caffeic acid 3-O-methyltransferase. Phytochemistry 65 (2004) 837-846
    • (2004) Phytochemistry , vol.65 , pp. 837-846
    • Kota, P.1    Guo, D.2    Zubieta, C.3    Noel, J.4    Dixon, R.A.5
  • 8
    • 0034163370 scopus 로고    scopus 로고
    • Substrate preferences of caffeic acid/5-hydroxyferulic acid/3-O-methyltransferases in developing stems of alfalfa (Medicago sativa L.)
    • Inoue K., Parvathi K., and Dixon R.A. Substrate preferences of caffeic acid/5-hydroxyferulic acid/3-O-methyltransferases in developing stems of alfalfa (Medicago sativa L.). Arch. Biochem. Biophys. 375 (2000) 175-182
    • (2000) Arch. Biochem. Biophys. , vol.375 , pp. 175-182
    • Inoue, K.1    Parvathi, K.2    Dixon, R.A.3
  • 9
    • 0035143813 scopus 로고    scopus 로고
    • Substrate preferences of O-methyltransferases in alfalfa suggest new pathways for 3-O-methylation of monolignols
    • Kota P., Chen F., Guo D., Blount J.W., and Dixon R.A. Substrate preferences of O-methyltransferases in alfalfa suggest new pathways for 3-O-methylation of monolignols. Plant J. 25 (2001) 193-202
    • (2001) Plant J. , vol.25 , pp. 193-202
    • Kota, P.1    Chen, F.2    Guo, D.3    Blount, J.W.4    Dixon, R.A.5
  • 10
    • 0033167045 scopus 로고    scopus 로고
    • Secondary xylem-specific expression of caffeoyl-coenzyme A 3-O-methyltransferase plays an important role in the methylation pathway associated with lignin biosynthesis in loblolly pine
    • Li L., Osakabe Y., Joshi C.P., and Chiang V.L. Secondary xylem-specific expression of caffeoyl-coenzyme A 3-O-methyltransferase plays an important role in the methylation pathway associated with lignin biosynthesis in loblolly pine. Plant Mol. Biol. 40 (1999) 555-565
    • (1999) Plant Mol. Biol. , vol.40 , pp. 555-565
    • Li, L.1    Osakabe, Y.2    Joshi, C.P.3    Chiang, V.L.4
  • 11
    • 0034054073 scopus 로고    scopus 로고
    • 5-Hydroxyconiferyl aldehyde modulates enzymatic methylation for syringyl monolignol formation: a new view of monolignol biosynthesis in angiosperms
    • Li L., Popko J.L., Umezawa T., and Chiang V.L. 5-Hydroxyconiferyl aldehyde modulates enzymatic methylation for syringyl monolignol formation: a new view of monolignol biosynthesis in angiosperms. J. Biol. Chem. 275 (2000) 6537-6545
    • (2000) J. Biol. Chem. , vol.275 , pp. 6537-6545
    • Li, L.1    Popko, J.L.2    Umezawa, T.3    Chiang, V.L.4
  • 12
    • 0035983842 scopus 로고    scopus 로고
    • Structural basis for the modulation of lignin monomer methylation by caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase
    • Zubieta C., Kota P., Ferrer J.-L., Dixon R.A., and Noel J. Structural basis for the modulation of lignin monomer methylation by caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase. Plant Cell 14 (2002) 1265-1277
    • (2002) Plant Cell , vol.14 , pp. 1265-1277
    • Zubieta, C.1    Kota, P.2    Ferrer, J.-L.3    Dixon, R.A.4    Noel, J.5
  • 13
    • 0031847268 scopus 로고    scopus 로고
    • Characterization of S-adenosyl-l-methionine: (Iso)eugenol-O-methyltransferase involved in floral scent production in Clarkia breweri
    • Wang J., and Pichersky E. Characterization of S-adenosyl-l-methionine: (Iso)eugenol-O-methyltransferase involved in floral scent production in Clarkia breweri. Arch. Biochem. Biophys. 349 (1998) 153-160
    • (1998) Arch. Biochem. Biophys. , vol.349 , pp. 153-160
    • Wang, J.1    Pichersky, E.2
  • 14
    • 0036009782 scopus 로고    scopus 로고
    • Characterization of phenylpropene O-methyltransferases from sweet basil: facile change of substrate specificity and convergent evolution within a plant O-methyltransferase family
    • Gang D.R., Lavid N., Zubieta C., Chen F., Beuerle T., Lewinsohn E., Noel J.P., and Pichersky E. Characterization of phenylpropene O-methyltransferases from sweet basil: facile change of substrate specificity and convergent evolution within a plant O-methyltransferase family. Plant Cell 14 (2002) 505-519
    • (2002) Plant Cell , vol.14 , pp. 505-519
    • Gang, D.R.1    Lavid, N.2    Zubieta, C.3    Chen, F.4    Beuerle, T.5    Lewinsohn, E.6    Noel, J.P.7    Pichersky, E.8
  • 15
    • 33750428586 scopus 로고    scopus 로고
    • Functional analysis of members of the isoflavone- and isoflavanone-O-methyltransferase gene families from the model legume Medicago truncatula
    • Deavours B.E., Liu C.-J., Naoumkina M.A., Tang Y., Farag M.A., Sumner L.W., Noel J.P., and Dixon R.A. Functional analysis of members of the isoflavone- and isoflavanone-O-methyltransferase gene families from the model legume Medicago truncatula. Plant Mol. Biol. 62 (2006) 715-733
    • (2006) Plant Mol. Biol. , vol.62 , pp. 715-733
    • Deavours, B.E.1    Liu, C.-J.2    Naoumkina, M.A.3    Tang, Y.4    Farag, M.A.5    Sumner, L.W.6    Noel, J.P.7    Dixon, R.A.8
  • 16
    • 0033083604 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of O-methyltransferases common to isoquinoline alkaloid and phenylpropanoid biosynthesis
    • Frick S., and Kutchan T.M. Molecular cloning and functional expression of O-methyltransferases common to isoquinoline alkaloid and phenylpropanoid biosynthesis. Plant J. 17 (1999) 329-339
    • (1999) Plant J. , vol.17 , pp. 329-339
    • Frick, S.1    Kutchan, T.M.2
  • 17
    • 0842303035 scopus 로고    scopus 로고
    • An enzyme-coupled colorimetric assay for S-adenosylmethionine-dependent methyltransferases
    • Hendricks C.L., Ross J.R., Pichersky E., Noel J.P., and Zhou Z.S. An enzyme-coupled colorimetric assay for S-adenosylmethionine-dependent methyltransferases. Anal. Biochem. 326 (2004) 100-105
    • (2004) Anal. Biochem. , vol.326 , pp. 100-105
    • Hendricks, C.L.1    Ross, J.R.2    Pichersky, E.3    Noel, J.P.4    Zhou, Z.S.5
  • 18
    • 20444414511 scopus 로고    scopus 로고
    • A coupled fluorescent assay for histone methyltransferases
    • Collazo E., Couture J.F., Bulfer S., and Trievel R.C. A coupled fluorescent assay for histone methyltransferases. Anal. Biochem. 342 (2005) 86-92
    • (2005) Anal. Biochem. , vol.342 , pp. 86-92
    • Collazo, E.1    Couture, J.F.2    Bulfer, S.3    Trievel, R.C.4
  • 20
    • 0036784071 scopus 로고    scopus 로고
    • Kinetics and crystal structure of catechol O-methyltransferase complex with co-substrate and a novel inhibitor with potential therapeutic application
    • Bonifacio M.J., Archer M., Rodrigues M.L., Matias P.M., Learmonth D.A., Carrondo M.A., and Soares-Da Silva P. Kinetics and crystal structure of catechol O-methyltransferase complex with co-substrate and a novel inhibitor with potential therapeutic application. Mol. Pharmacol. 62 (2002) 795-805
    • (2002) Mol. Pharmacol. , vol.62 , pp. 795-805
    • Bonifacio, M.J.1    Archer, M.2    Rodrigues, M.L.3    Matias, P.M.4    Learmonth, D.A.5    Carrondo, M.A.6    Soares-Da Silva, P.7
  • 21
    • 33947534869 scopus 로고    scopus 로고
    • Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses
    • Liu C.-J., Deavours B.E., Richard S.B., Ferrer J.-L., Blount J.W., Huhman D., Dixon R.A., and Noel J.P. Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses. Plant Cell 18 (2006) 3656-3669
    • (2006) Plant Cell , vol.18 , pp. 3656-3669
    • Liu, C.-J.1    Deavours, B.E.2    Richard, S.B.3    Ferrer, J.-L.4    Blount, J.W.5    Huhman, D.6    Dixon, R.A.7    Noel, J.P.8
  • 22
    • 0000370798 scopus 로고
    • Phenol test III: the indophenol test
    • Gibbs H.D. Phenol test III: the indophenol test. J. Biol. Chem. 72 (1927) 649-664
    • (1927) J. Biol. Chem. , vol.72 , pp. 649-664
    • Gibbs, H.D.1
  • 23
    • 0000915657 scopus 로고
    • Reaction of Gibbs reagent with para-substituted phenols
    • Josephy P.D., and Damme A.V. Reaction of Gibbs reagent with para-substituted phenols. Anal. Chem. 56 (1984) 813-814
    • (1984) Anal. Chem. , vol.56 , pp. 813-814
    • Josephy, P.D.1    Damme, A.V.2
  • 24
    • 0000698573 scopus 로고
    • Nonspecificity of Gibbs' reagent
    • Dacre J.C. Nonspecificity of Gibbs' reagent. Anal. Chem. 43 (1971) 589-591
    • (1971) Anal. Chem. , vol.43 , pp. 589-591
    • Dacre, J.C.1
  • 26
    • 47749146143 scopus 로고    scopus 로고
    • Nucleocytoplasmic-localized acyltransferases catalyze the malonylation of 7-O-glycosidic (iso)flavones in Medicago truncatula
    • Yu X.H., Chen M.H., and Liu C.J. Nucleocytoplasmic-localized acyltransferases catalyze the malonylation of 7-O-glycosidic (iso)flavones in Medicago truncatula. Plant J. 55 (2008) 382-396
    • (2008) Plant J. , vol.55 , pp. 382-396
    • Yu, X.H.1    Chen, M.H.2    Liu, C.J.3
  • 27
    • 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. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 33749452178 scopus 로고    scopus 로고
    • Development of an analytical method for genome-wide functional identification of plant acyl-CoA dependent acyltransferases
    • Yu X.-H., and Liu C.-J. Development of an analytical method for genome-wide functional identification of plant acyl-CoA dependent acyltransferases. Anal. Biochem. 358 (2006) 146-148
    • (2006) Anal. Biochem. , vol.358 , pp. 146-148
    • Yu, X.-H.1    Liu, C.-J.2
  • 30
    • 0030792380 scopus 로고    scopus 로고
    • Colorimetric method for a rapid detection of oxygenated aromatic biotransformation products
    • Quintana M.G., Didion C., and Dalton H. Colorimetric method for a rapid detection of oxygenated aromatic biotransformation products. Biotechnol. Tech. 11 (1997) 585-587
    • (1997) Biotechnol. Tech. , vol.11 , pp. 585-587
    • Quintana, M.G.1    Didion, C.2    Dalton, H.3


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