메뉴 건너뛰기




Volumn 1850, Issue 7, 2015, Pages 1405-1414

Active site cleft mutants of Os9BGlu31 transglucosidase modify acceptor substrate specificity and allow production of multiple kaempferol glycosides

Author keywords

Electrospray ionization mass spectrometry; Glycoside hydrolase family GH1; Glycosylation; Rice (Oryza sativa L.); Site directed mutagenesis; Transglucosidase

Indexed keywords

4 NITROPHENYL BETA DEXTRO GLUCOPYRANOSIDE; ASTRAGALIN; GLUCOPYRANOSIDE; GLUCOSIDASE; GLYCOSIDE; HYDROXYL GROUP; KAEMPFEROL; KAEMPFEROL 4 O GLUCOSIDE; KAEMPFEROL 7 O GLYCOSIDE; UNCLASSIFIED DRUG; KAEMPFEROL DERIVATIVE; KAEMPFEROL-3-O-GLUCOSIDE; MONOSACCHARIDE; MUTANT PROTEIN; VEGETABLE PROTEIN;

EID: 84942693641     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2015.03.013     Document Type: Article
Times cited : (11)

References (34)
  • 2
    • 84890293759 scopus 로고    scopus 로고
    • A novel integrated method for large-scale detection, identification and quantification of widely-targeted metabolites: Application in study of rice metabolomics
    • C. Wei, G. Liang, G. Zilong, W. Wensheng, Z. Hongyan, L. Xianqing, Y. Sibin, X. Lizhong, and L. Jie A novel integrated method for large-scale detection, identification and quantification of widely-targeted metabolites: application in study of rice metabolomics Mol. Plant 6 6 2013 1769 1780
    • (2013) Mol. Plant , vol.6 , Issue.6 , pp. 1769-1780
    • Wei, C.1    Liang, G.2    Zilong, G.3    Wensheng, W.4    Hongyan, Z.5    Xianqing, L.6    Sibin, Y.7    Lizhong, X.8    Jie, L.9
  • 3
    • 9144219793 scopus 로고    scopus 로고
    • Mechanistic analogies amongst carbohydrate modifying enzymes
    • L.L. Lairson, and S.G. Withers Mechanistic analogies amongst carbohydrate modifying enzymes Chem. Commun. 2004 2243 2248
    • (2004) Chem. Commun. , pp. 2243-2248
    • Lairson, L.L.1    Withers, S.G.2
  • 8
    • 84876167278 scopus 로고    scopus 로고
    • Glycosynthase with broad substrate specificity-an efficient biocatalyst for the construction of oligosaccharide library
    • J. Wei, X. Lv, Y. Lu, G. Yang, L. Fu, L. Yang, J. Wang, J. Gao, S. Cheng, Q. Duan, C. Jin, and X. Li Glycosynthase with broad substrate specificity-an efficient biocatalyst for the construction of oligosaccharide library Eur. J. Org. Chem. 138 2013 2412 2419
    • (2013) Eur. J. Org. Chem. , vol.138 , pp. 2412-2419
    • Wei, J.1    Lv, X.2    Lu, Y.3    Yang, G.4    Fu, L.5    Yang, L.6    Wang, J.7    Gao, J.8    Cheng, S.9    Duan, Q.10    Jin, C.11    Li, X.12
  • 9
    • 0348209612 scopus 로고    scopus 로고
    • Thioglycoligases: Mutant glycosidases for thioglycoside synthesis
    • M. Jahn, J. Marles, R.A.J. Warren, and S.G. Withers Thioglycoligases: mutant glycosidases for thioglycoside synthesis Angew. Chem. Int. Ed. 42 2003 532 534
    • (2003) Angew. Chem. Int. Ed. , vol.42 , pp. 532-534
    • Jahn, M.1    Marles, J.2    Warren, R.A.J.3    Withers, S.G.4
  • 10
    • 33750006508 scopus 로고    scopus 로고
    • Direct evolution an approach to engineer enzymes
    • J. Kaur, and R. Sharma Direct evolution an approach to engineer enzymes Crit. Rev. Biotechnol. 26 2006 165 199
    • (2006) Crit. Rev. Biotechnol. , vol.26 , pp. 165-199
    • Kaur, J.1    Sharma, R.2
  • 11
    • 34547657101 scopus 로고    scopus 로고
    • Structural evidence for the evolution of xyloglucanase activity from xyloglucan endo-transglycosylases: Biological implications for cell wall metabolism
    • M.J. Baumann, J.M. Eklöf, G. Michel, Åsa M. Kalla, T.T. Teeri, M. Czjzek, and H. Brumer III Structural evidence for the evolution of xyloglucanase activity from xyloglucan endo-transglycosylases: biological implications for cell wall metabolism Plant Cell 19 2007 1947 1963
    • (2007) Plant Cell , vol.19 , pp. 1947-1963
    • Baumann, M.J.1    Eklof, J.M.2    Michel, G.3    Kalla, A.M.4    Teeri, T.T.5    Czjzek, M.6    Brumer, H.7
  • 12
    • 79751533015 scopus 로고    scopus 로고
    • Galactoglycerolipid metabolism under stress: A time for remodeling
    • E.R. Moellering, and C. Benning Galactoglycerolipid metabolism under stress: a time for remodeling Trends Plant Sci. 16 2010 98 107
    • (2010) Trends Plant Sci. , vol.16 , pp. 98-107
    • Moellering, E.R.1    Benning, C.2
  • 13
    • 84888396457 scopus 로고    scopus 로고
    • P-Hydroxybenzoyl-glucose is a zwitter donor for the biosynthesis of 7-poly acylated anthocyanin in delphinium
    • Y. Nishizaki, M. Yasunaga, E. Okamoto, M. Okamoto, Y. Hirose, M. Yamaguchi, Y. Ozeki, and N. Sasaki p-Hydroxybenzoyl-glucose is a zwitter donor for the biosynthesis of 7-poly acylated anthocyanin in delphinium Plant Cell 25 2013 4150 4165
    • (2013) Plant Cell , vol.25 , pp. 4150-4165
    • Nishizaki, Y.1    Yasunaga, M.2    Okamoto, E.3    Okamoto, M.4    Hirose, Y.5    Yamaguchi, M.6    Ozeki, Y.7    Sasaki, N.8
  • 14
    • 84875068820 scopus 로고    scopus 로고
    • Acyl-glucose-dependent glucosyltransferase catalyzes the final step of anthocyanin formation in Arabidopsis
    • T. Miyahara, R. Sakiyama, Y. Ozeki, and N. Sasaki Acyl-glucose-dependent glucosyltransferase catalyzes the final step of anthocyanin formation in Arabidopsis J. Plant Physiol. 170 2013 619 624
    • (2013) J. Plant Physiol. , vol.170 , pp. 619-624
    • Miyahara, T.1    Sakiyama, R.2    Ozeki, Y.3    Sasaki, N.4
  • 17
    • 0031864258 scopus 로고    scopus 로고
    • Structure-activity relationships for antioxidant activities of a series of flavonoids in a liposomal system
    • A. Arora, M.G. Nair, and M.G. Strasburg Structure-activity relationships for antioxidant activities of a series of flavonoids in a liposomal system Free Radic. Biol. Med. 24 1998 13 55
    • (1998) Free Radic. Biol. Med. , vol.24 , pp. 13-55
    • Arora, A.1    Nair, M.G.2    Strasburg, M.G.3
  • 19
    • 84863670193 scopus 로고    scopus 로고
    • Simultaneous determination of phenolic acids and flavonoids in rice using solid-phase extraction and RP-HPLC with photodiode array detection
    • M.N. Irakli, V.F. Samanidou, C.G. Biliaderis, and I.N. Papadoyannis Simultaneous determination of phenolic acids and flavonoids in rice using solid-phase extraction and RP-HPLC with photodiode array detection J. Sep. Sci. 35 2012 1603 1611
    • (2012) J. Sep. Sci. , vol.35 , pp. 1603-1611
    • Irakli, M.N.1    Samanidou, V.F.2    Biliaderis, C.G.3    Papadoyannis, I.N.4
  • 20
    • 80054030651 scopus 로고    scopus 로고
    • LC/MS profiling of flavonoid glycoconjugates isolated from hairy roots, suspension root cell cultures and seedling roots of Medicago truncatula
    • A. Staszków, B. Swarcewicz, J. Banasiak, D. Muth, M. Jasiński, and M. Stobiecki LC/MS profiling of flavonoid glycoconjugates isolated from hairy roots, suspension root cell cultures and seedling roots of Medicago truncatula Metabolomics 7 2011 604 613
    • (2011) Metabolomics , vol.7 , pp. 604-613
    • Staszków, A.1    Swarcewicz, B.2    Banasiak, J.3    Muth, D.4    Jasiński, M.5    Stobiecki, M.6
  • 21
    • 0037260750 scopus 로고    scopus 로고
    • Studying of the collision-induced radical cleavage of flavonoid glycosides using negative electrospray ionization tandem quadrupole mass spectrometry
    • E. Hvattum, and D. Ekeberg Studying of the collision-induced radical cleavage of flavonoid glycosides using negative electrospray ionization tandem quadrupole mass spectrometry J. Mass Spectrom. 38 2003 43 49
    • (2003) J. Mass Spectrom. , vol.38 , pp. 43-49
    • Hvattum, E.1    Ekeberg, D.2
  • 22
    • 4344675430 scopus 로고    scopus 로고
    • LC-DAD UV and LC-MS for the analysis of isoflavonoids and flavones from in vitro and in vivo biomass of Genista tinctoria L
    • M. Luczkiewicz, D. Glod, and T.A. Bucinski LC-DAD UV and LC-MS for the analysis of isoflavonoids and flavones from in vitro and in vivo biomass of Genista tinctoria L Chromatographia 60 2004 179 185
    • (2004) Chromatographia , vol.60 , pp. 179-185
    • Luczkiewicz, M.1    Glod, D.2    Bucinski, T.A.3
  • 23
    • 0035567362 scopus 로고    scopus 로고
    • Determination of flavone, flavonol, and flavonone aglycones by negative ion liquid chromatography electrospray ion trap mass spectrometry
    • N. Fabre, I. Rustan, E. de Hoffmann, and J. Quetin-Leclercq Determination of flavone, flavonol, and flavonone aglycones by negative ion liquid chromatography electrospray ion trap mass spectrometry J. Am. Soc. Mass Spectrom. 12 2001 707 715
    • (2001) J. Am. Soc. Mass Spectrom. , vol.12 , pp. 707-715
    • Fabre, N.1    Rustan, I.2    De Hoffmann, E.3    Quetin-Leclercq, J.4
  • 24
    • 1142303819 scopus 로고    scopus 로고
    • Mass spectrometry in the structural analysis of flavonoids
    • F. Cuyckens, and M. Claeys Mass spectrometry in the structural analysis of flavonoids J. Mass Spectrom. 39 2004 1 15
    • (2004) J. Mass Spectrom. , vol.39 , pp. 1-15
    • Cuyckens, F.1    Claeys, M.2
  • 25
    • 84870371475 scopus 로고    scopus 로고
    • Quantification of flavonoids in black rice by liquid chromatography negative electrospray ionization tandem mass spectrometry
    • T. Sinseadka, S. Wongpornchai, and M. Rayanakorn Quantification of flavonoids in black rice by liquid chromatography negative electrospray ionization tandem mass spectrometry J. Agric. Food Chem. 60 2010 11723 11732
    • (2010) J. Agric. Food Chem. , vol.60 , pp. 11723-11732
    • Sinseadka, T.1    Wongpornchai, S.2    Rayanakorn, M.3
  • 26
    • 33645517905 scopus 로고    scopus 로고
    • Structuralcharacterization of flavonol 3,7-di-O-glycosides and determination of the glycosylation position by using negative ion electrospray ionization tandem mass spectrometry
    • K. Ablajan, Z. Abliz, X.Y. Shang, J.M. He, R.P. Zhang, and J.G. Shi Structuralcharacterization of flavonol 3,7-di-O-glycosides and determination of the glycosylation position by using negative ion electrospray ionization tandem mass spectrometry J. Mass Spectrom. 41 2006 352 360
    • (2006) J. Mass Spectrom. , vol.41 , pp. 352-360
    • Ablajan, K.1    Abliz, Z.2    Shang, X.Y.3    He, J.M.4    Zhang, R.P.5    Shi, J.G.6
  • 27
    • 0042130165 scopus 로고    scopus 로고
    • Characterization of a rice β-glucosidase genes highly expressed in flower and germinating shoot
    • R. Opassiri, J.R. Ketudat Cairns, T. Akiyama, O. Wara-Aswapati, J. Svasti, and A. Esen Characterization of a rice β-glucosidase genes highly expressed in flower and germinating shoot Plant Sci. 165 2003 627 638
    • (2003) Plant Sci. , vol.165 , pp. 627-638
    • Opassiri, R.1    Ketudat Cairns, J.R.2    Akiyama, T.3    Wara-Aswapati, O.4    Svasti, J.5    Esen, A.6
  • 28
    • 70349221692 scopus 로고    scopus 로고
    • Structural and enzymatic characterization of Os3BGlu6, a rice β-glucosidase hydrolyzing hydrophobic glycosides and (1→3)- and (1→2)-linked disaccharides
    • S. Seshadri, T. Akiyama, R. Opassiri, B. Kuaprasert, and J.R. Ketudat Cairns Structural and enzymatic characterization of Os3BGlu6, a rice β-glucosidase hydrolyzing hydrophobic glycosides and (1→3)- and (1→2)-linked disaccharides Plant Physiol. 151 2009 47 58
    • (2009) Plant Physiol. , vol.151 , pp. 47-58
    • Seshadri, S.1    Akiyama, T.2    Opassiri, R.3    Kuaprasert, B.4    Ketudat Cairns, J.R.5
  • 31
    • 84858075955 scopus 로고    scopus 로고
    • Exchanging a single amino acid residue generates or weakens a + 2 cello-oligosaccharide binding subsite in rice β-glucosidases
    • S. Sansenya, J. Maneesan, and J.R. Ketudat Cairns Exchanging a single amino acid residue generates or weakens a + 2 cello-oligosaccharide binding subsite in rice β-glucosidases Carbohydr. Res. 351 2012 130 133
    • (2012) Carbohydr. Res. , vol.351 , pp. 130-133
    • Sansenya, S.1    Maneesan, J.2    Ketudat Cairns, J.R.3
  • 33
    • 84928949306 scopus 로고    scopus 로고
    • Effects of active site cleft residues on oligosaccharide binding, hydrolysis and glycosynthase activities of rice BGlu1 and its mutants
    • S. Pengthaisong, and J.R. Ketudat Cairns Effects of active site cleft residues on oligosaccharide binding, hydrolysis and glycosynthase activities of rice BGlu1 and its mutants Protein Sci. 23 2014 1738 1752
    • (2014) Protein Sci. , vol.23 , pp. 1738-1752
    • Pengthaisong, S.1    Ketudat Cairns, J.R.2
  • 34
    • 0034610330 scopus 로고    scopus 로고
    • He mechanism of substrate (aglycone) specificity in beta-glucosidases is revealed by crystal structures of mutant maize beta-glucosidase-DIMBOA, -DIMBOAGlc and -dhurrin complexes
    • M. Czjzek, M. Cicek, V. Zamboni, D.R. Bevan, B. Henrissat, and A. Esen he mechanism of substrate (aglycone) specificity in beta-glucosidases is revealed by crystal structures of mutant maize beta-glucosidase-DIMBOA, -DIMBOAGlc and -dhurrin complexes Proc. Natl. Acad. Sci. U. S. A. 97 2000 13555 13560
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 13555-13560
    • Czjzek, M.1    Cicek, M.2    Zamboni, V.3    Bevan, D.R.4    Henrissat, B.5    Esen, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.