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Volumn 191-192, Issue , 2012, Pages 82-92

Properties of β-thioglucoside hydrolases (TGG1 and TGG2) from leaves of Arabidopsis thaliana

Author keywords

Arabidopsis thaliana; Brassicaceae; Deglycosylation; Glucosinolate; Myrosinase; Protein purification

Indexed keywords

ARABIDOPSIS PROTEIN; ASCORBIC ACID; GLYCOSIDASE; PEPTIDE; TGG1 PROTEIN, ARABIDOPSIS; TGG2 PROTEIN, ARABIDOPSIS; THIOGLUCOSIDASE;

EID: 84861217871     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2012.02.004     Document Type: Article
Times cited : (35)

References (44)
  • 1
    • 0034671719 scopus 로고    scopus 로고
    • High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base
    • Burmeister W.P., Cottaz S., Rollin P., Vasella A., Henrissat B. High resolution X-ray crystallography shows that ascorbate is a cofactor for myrosinase and substitutes for the function of the catalytic base. J. Biol. Chem. 2000, 275:39385-39393.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39385-39393
    • Burmeister, W.P.1    Cottaz, S.2    Rollin, P.3    Vasella, A.4    Henrissat, B.5
  • 2
  • 3
    • 0035177447 scopus 로고    scopus 로고
    • Purification and characterisation of a non-plant myrosinase from the cabbage aphid Brevicoryne brassicae (L.)
    • Jones A.M.E., Bridges M., Bones A.M., Cole R., Rossiter J.T. Purification and characterisation of a non-plant myrosinase from the cabbage aphid Brevicoryne brassicae (L.). Insect Biochem. Mol. Biol. 2001, 31:1-5.
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 1-5
    • Jones, A.M.E.1    Bridges, M.2    Bones, A.M.3    Cole, R.4    Rossiter, J.T.5
  • 4
    • 0035055610 scopus 로고    scopus 로고
    • Purification and characterization of myrosinase from the cabbage aphid (Brevicoryne brassicae), a brassica herbivore
    • Pontoppidan P., Ekbom B., Eriksson S., Meijer J. Purification and characterization of myrosinase from the cabbage aphid (Brevicoryne brassicae), a brassica herbivore. Eur. J. Biochem. 2001, 268:1041-1048.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1041-1048
    • Pontoppidan, P.1    Ekbom, B.2    Eriksson, S.3    Meijer, J.4
  • 9
    • 0015527327 scopus 로고
    • Studies on myrosinases EC-3.2.3.1 I. Purification and characterization of a myrosinase from white mustard seed Sinapis alba
    • Björkman R., Janson J.-C. Studies on myrosinases EC-3.2.3.1 I. Purification and characterization of a myrosinase from white mustard seed Sinapis alba. Biochim. Biophys. Acta 1972, 276:508-518.
    • (1972) Biochim. Biophys. Acta , vol.276 , pp. 508-518
    • Björkman, R.1    Janson, J.-C.2
  • 10
    • 0001767954 scopus 로고
    • Molecular properties of multiple forms of plant myrosinase
    • Ohtsuru M., Hata T. Molecular properties of multiple forms of plant myrosinase. Agric. Biol. Chem. 1972, 36:2495-2503.
    • (1972) Agric. Biol. Chem. , vol.36 , pp. 2495-2503
    • Ohtsuru, M.1    Hata, T.2
  • 11
    • 0015798629 scopus 로고
    • Studies on myrosinases II. Purification and characterization of a myrosinase from rapeseed Brassica napus
    • Lönnerdal B., Janson J.-C. Studies on myrosinases II. Purification and characterization of a myrosinase from rapeseed Brassica napus. Biochim. Biophys. Acta 1973, 315:421-429.
    • (1973) Biochim. Biophys. Acta , vol.315 , pp. 421-429
    • Lönnerdal, B.1    Janson, J.-C.2
  • 12
    • 84952397604 scopus 로고
    • Studies on the myrosinase from Wasabia japonica: purification and some properties of wasabi myrosinase
    • Ohtsuru M., Kawatani H. Studies on the myrosinase from Wasabia japonica: purification and some properties of wasabi myrosinase. Agric. Biol. Chem. 1979, 43:2249-2255.
    • (1979) Agric. Biol. Chem. , vol.43 , pp. 2249-2255
    • Ohtsuru, M.1    Kawatani, H.2
  • 13
    • 33845373904 scopus 로고
    • Myrosinase from Sinapis alba L.: a new method purification for glucosinolate analyses
    • Palmieri S., Iori R., Leoni O. Myrosinase from Sinapis alba L.: a new method purification for glucosinolate analyses. J. Agric. Food Chem. 1986, 34:138-140.
    • (1986) J. Agric. Food Chem. , vol.34 , pp. 138-140
    • Palmieri, S.1    Iori, R.2    Leoni, O.3
  • 14
    • 0001873443 scopus 로고
    • Effect of castanospermine and related polyhydroxyalkaloids on purified myrosinase from Lepidium sativum seedlings
    • Durham P.L., Poulton J.E. Effect of castanospermine and related polyhydroxyalkaloids on purified myrosinase from Lepidium sativum seedlings. Plant Physiol. 1989, 90:48-52.
    • (1989) Plant Physiol. , vol.90 , pp. 48-52
    • Durham, P.L.1    Poulton, J.E.2
  • 15
    • 0033178510 scopus 로고    scopus 로고
    • An unusual case of 'uncompetitive activation' by ascorbic acid: purification and kinetic properties of a myrosinase from Raphanus sativus seedlings
    • Shikita M., Fahey J.W., Golden T.R., Holtzclaw W.D., Talalay P. An unusual case of 'uncompetitive activation' by ascorbic acid: purification and kinetic properties of a myrosinase from Raphanus sativus seedlings. Biochem. J. 1999, 341:725-732.
    • (1999) Biochem. J. , vol.341 , pp. 725-732
    • Shikita, M.1    Fahey, J.W.2    Golden, T.R.3    Holtzclaw, W.D.4    Talalay, P.5
  • 16
    • 0037462042 scopus 로고    scopus 로고
    • Isolation and biochemical characterization of a basic myrosinase from ripe Crambe abyssinica seeds, highly specific for epi-progoitrin
    • Bernardi R., Finiguerra M.G., Rossi A.A., Palmieri S. Isolation and biochemical characterization of a basic myrosinase from ripe Crambe abyssinica seeds, highly specific for epi-progoitrin. J. Agric. Food Chem. 2003, 51:2737-2744.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 2737-2744
    • Bernardi, R.1    Finiguerra, M.G.2    Rossi, A.A.3    Palmieri, S.4
  • 17
    • 0031570331 scopus 로고    scopus 로고
    • The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insights into the substrate recognition and active-site machinery of an S-glycosidase
    • Burmeister W.P., Cottaz S., Driguez H., Iori R., Palmieri S., Henrissat B. The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insights into the substrate recognition and active-site machinery of an S-glycosidase. Structure 1997, 5:663-675.
    • (1997) Structure , vol.5 , pp. 663-675
    • Burmeister, W.P.1    Cottaz, S.2    Driguez, H.3    Iori, R.4    Palmieri, S.5    Henrissat, B.6
  • 19
    • 70349453816 scopus 로고    scopus 로고
    • Myrosinases from root and leaves of Arabidopsis thaliana have different catalytic properties
    • Andersson D., Chakrabarty R., Bejai S., Zhang J.M., Rask L., Meijer J. Myrosinases from root and leaves of Arabidopsis thaliana have different catalytic properties. Phytochemistry 2009, 70:1345-1354.
    • (2009) Phytochemistry , vol.70 , pp. 1345-1354
    • Andersson, D.1    Chakrabarty, R.2    Bejai, S.3    Zhang, J.M.4    Rask, L.5    Meijer, J.6
  • 20
    • 0036258549 scopus 로고    scopus 로고
    • The third myrosinase gene TGG3 in Arabidopsis thaliana is a pseudogene specifically expressed in stamen and petal
    • Zhang J.M., Pontoppidan B., Xue J.P., Rask L., Meijer J. The third myrosinase gene TGG3 in Arabidopsis thaliana is a pseudogene specifically expressed in stamen and petal. Physiol. Plant. 2002, 115:25-34.
    • (2002) Physiol. Plant. , vol.115 , pp. 25-34
    • Zhang, J.M.1    Pontoppidan, B.2    Xue, J.P.3    Rask, L.4    Meijer, J.5
  • 21
    • 67749132420 scopus 로고    scopus 로고
    • The two non-functional myrosinase genes TGG3 and TGG6 in Arabidopsis are expressed predominantly in pollen
    • Wang M., Sun X.P., Tan D.G., Gong S.F., Meijer J., Zhang J.M. The two non-functional myrosinase genes TGG3 and TGG6 in Arabidopsis are expressed predominantly in pollen. Plant Sci. 2009, 177:371-375.
    • (2009) Plant Sci. , vol.177 , pp. 371-375
    • Wang, M.1    Sun, X.P.2    Tan, D.G.3    Gong, S.F.4    Meijer, J.5    Zhang, J.M.6
  • 22
    • 33646232241 scopus 로고    scopus 로고
    • Arabidopsis myrosinases TGG1 and TGG2 have redundant function in glucosinolate breakdown and insect defense
    • Barth C., Jander G. Arabidopsis myrosinases TGG1 and TGG2 have redundant function in glucosinolate breakdown and insect defense. Plant J. 2006, 46:549-562.
    • (2006) Plant J. , vol.46 , pp. 549-562
    • Barth, C.1    Jander, G.2
  • 23
    • 13644257223 scopus 로고    scopus 로고
    • Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites
    • Julenius K., Molgaard A., Gupta R., Brunak S. Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites. Glycobiology 2005, 15:153-164.
    • (2005) Glycobiology , vol.15 , pp. 153-164
    • Julenius, K.1    Molgaard, A.2    Gupta, R.3    Brunak, S.4
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0029645413 scopus 로고
    • The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase
    • Barrett T., Suresh C., Tolley S., Dodson E., Hughes M. The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase. Structure 1995, 3:951-960.
    • (1995) Structure , vol.3 , pp. 951-960
    • Barrett, T.1    Suresh, C.2    Tolley, S.3    Dodson, E.4    Hughes, M.5
  • 30
    • 85007985341 scopus 로고
    • Studies on myrosinase in mustard seed Part V On the β-glucosidase activity of myrosinase and the interaction of ascorbate with myrosinase
    • Tsuruo I., Hata T. Studies on myrosinase in mustard seed Part V On the β-glucosidase activity of myrosinase and the interaction of ascorbate with myrosinase. Agric. Biol. Chem. 1968, 32:1425.
    • (1968) Agric. Biol. Chem. , vol.32 , pp. 1425
    • Tsuruo, I.1    Hata, T.2
  • 32
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • Henrissat B., Davies G. Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol. 1997, 7:637-644.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 34
    • 27744530037 scopus 로고    scopus 로고
    • Crystal structure at 1.1angstrom resolution of an insect myrosinase from Brevicoryne brassicae shows its close relationship to β glucosidases
    • Husebye H., Arzt S., Burmeister W.P., Härtel F.V., Brandt A., Rossiter J.T., Bones A.M. Crystal structure at 1.1angstrom resolution of an insect myrosinase from Brevicoryne brassicae shows its close relationship to β glucosidases. Insect Biochem. Mol. Biol. 2005, 35:1311-1320.
    • (2005) Insect Biochem. Mol. Biol. , vol.35 , pp. 1311-1320
    • Husebye, H.1    Arzt, S.2    Burmeister, W.P.3    Härtel, F.V.4    Brandt, A.5    Rossiter, J.T.6    Bones, A.M.7
  • 35
    • 0000295679 scopus 로고    scopus 로고
    • The myrosinase-glucosinolate system, its organisation and biochemistry
    • Bones A.M., Rossiter J.T. The myrosinase-glucosinolate system, its organisation and biochemistry. Physiol. Plant. 1996, 97:194-208.
    • (1996) Physiol. Plant. , vol.97 , pp. 194-208
    • Bones, A.M.1    Rossiter, J.T.2
  • 38
    • 22344435238 scopus 로고    scopus 로고
    • Inhibition of soil-borne plant pathogens by the treatment of sinigrin and myrosinases released from reconstructed Escherichia coli and Pichia pastoris
    • Chung W.C., Huang H.C., Chiang B.T., Huang J.W. Inhibition of soil-borne plant pathogens by the treatment of sinigrin and myrosinases released from reconstructed Escherichia coli and Pichia pastoris. Biocontrol Sci. Technol. 2005, 15:455-465.
    • (2005) Biocontrol Sci. Technol. , vol.15 , pp. 455-465
    • Chung, W.C.1    Huang, H.C.2    Chiang, B.T.3    Huang, J.W.4
  • 39
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius A., Aebi M. Roles of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem. 2004, 73:1019-1049.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 40
    • 0000180578 scopus 로고
    • Protease inhibitors in plants: genes for improving defenses against insects and pathogens
    • Ryan C.A. Protease inhibitors in plants: genes for improving defenses against insects and pathogens. Annu. Rev. Phytopathol. 1990, 28:425-449.
    • (1990) Annu. Rev. Phytopathol. , vol.28 , pp. 425-449
    • Ryan, C.A.1
  • 42
    • 77951249123 scopus 로고    scopus 로고
    • Defence mechanisms of Brassicaceae: implications for plant-insect interactions and potential for integrated pest management. A review
    • Ahuja I., Rohloff J., Bones A.M. Defence mechanisms of Brassicaceae: implications for plant-insect interactions and potential for integrated pest management. A review. Agron. Sust. Dev. 2010, 30:311-348.
    • (2010) Agron. Sust. Dev. , vol.30 , pp. 311-348
    • Ahuja, I.1    Rohloff, J.2    Bones, A.M.3
  • 43
    • 0024187724 scopus 로고
    • Saturniid and sphingid caterpillars: two ways to eat leaves
    • Bernays E.A., Janzen D.H. Saturniid and sphingid caterpillars: two ways to eat leaves. Ecology 1988, 69:1153-1160.
    • (1988) Ecology , vol.69 , pp. 1153-1160
    • Bernays, E.A.1    Janzen, D.H.2
  • 44
    • 37349017552 scopus 로고    scopus 로고
    • The biomechanics of chewing and plant fracture: mechanisms and implications
    • Clissold F.J. The biomechanics of chewing and plant fracture: mechanisms and implications. Insect Mech. Control 2008, 317-372.
    • (2008) Insect Mech. Control , pp. 317-372
    • Clissold, F.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.