메뉴 건너뛰기




Volumn 1774, Issue 3, 2007, Pages 392-402

Purification and physico-kinetic characterization of 3β-hydroxy specific sterol glucosyltransferase from Withania somnifera (L) and its stress response

Author keywords

Heat stress; Salicylic acid signal; Sterol glucoside; Sterol glucosyltransferase; Stress response; Substrate specificity; Withanosides

Indexed keywords

24 METHYLENE CHOLESTEROL; AGLYCONE; CHOLESTEROL DERIVATIVE; FLAVONOID; GLUCOSYLTRANSFERASE; GLYCOSIDE; HYDROXYL GROUP; ISOFLAVONOID; PHYTOSTEROL; SALICYLIC ACID; STEROL GLUCOSYLTRANSFERASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCOSE; VEGETABLE PROTEIN; WITHANOLIDE;

EID: 33847659963     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.12.009     Document Type: Article
Times cited : (39)

References (45)
  • 2
    • 0032521608 scopus 로고    scopus 로고
    • Purification and kinetic analysis of a baculovirus ecdysteroid UDP-glucosyltransferase
    • Evans O.P., and O'reilly D.R. Purification and kinetic analysis of a baculovirus ecdysteroid UDP-glucosyltransferase. Biochem. J. 330 (1998) 1265-1270
    • (1998) Biochem. J. , vol.330 , pp. 1265-1270
    • Evans, O.P.1    O'reilly, D.R.2
  • 3
    • 0031026232 scopus 로고    scopus 로고
    • Heat stress induces a glycosylation of membrane sterol in myxoamoeba of a true slime mold, Physarum polycephalum
    • Murakami-Murofushi K., Nishikawa K., Hirakawa E., and Murofushi H. Heat stress induces a glycosylation of membrane sterol in myxoamoeba of a true slime mold, Physarum polycephalum. J. Biol. Chem. 272 (1997) 486-489
    • (1997) J. Biol. Chem. , vol.272 , pp. 486-489
    • Murakami-Murofushi, K.1    Nishikawa, K.2    Hirakawa, E.3    Murofushi, H.4
  • 4
    • 0034141687 scopus 로고    scopus 로고
    • Brasinosteroid signal transduction: still casting the actors
    • Schumacher K., and Chory J. Brasinosteroid signal transduction: still casting the actors. Curr. Opin. Plant Biol. 3 (2000) 79-84
    • (2000) Curr. Opin. Plant Biol. , vol.3 , pp. 79-84
    • Schumacher, K.1    Chory, J.2
  • 6
    • 0035753787 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis via 1-deoxy-d-xylulose-5-phosphate 2-C-methyl-d-erythritol 4-phosphate (DOXP/ MEP) pathway
    • Wanke M., Skorupinska-Tudek K., and Swiezewska E. Isoprenoid biosynthesis via 1-deoxy-d-xylulose-5-phosphate 2-C-methyl-d-erythritol 4-phosphate (DOXP/ MEP) pathway. Acta Biochim. Pol. 48 (2001) 663-672
    • (2001) Acta Biochim. Pol. , vol.48 , pp. 663-672
    • Wanke, M.1    Skorupinska-Tudek, K.2    Swiezewska, E.3
  • 8
    • 0027366574 scopus 로고
    • UDP-glucose sterol-β-d-glucosyltransferase, a plasma membrane bound enzyme of plants: enzymatic properties and lipid dependence
    • Ullmann P., Ury A., Rimmele D., Benveniste P., and Bouvier-Nave P. UDP-glucose sterol-β-d-glucosyltransferase, a plasma membrane bound enzyme of plants: enzymatic properties and lipid dependence. Biochimie 75 (1993) 713-719
    • (1993) Biochimie , vol.75 , pp. 713-719
    • Ullmann, P.1    Ury, A.2    Rimmele, D.3    Benveniste, P.4    Bouvier-Nave, P.5
  • 10
    • 0003086024 scopus 로고
    • Effect of sterylglycosides on the phase transition of dipalmitoyl lecithin
    • Mudd J.B., and McManus T.T. Effect of sterylglycosides on the phase transition of dipalmitoyl lecithin. Plant Physiol. 65 (1980) 78-80
    • (1980) Plant Physiol. , vol.65 , pp. 78-80
    • Mudd, J.B.1    McManus, T.T.2
  • 11
    • 0028849110 scopus 로고
    • Effect of plant sterols on the hydration and phase behavior of DOPE/DOPC mixtures
    • Webb M.S., Irving T.C., and Steponkus P.L. Effect of plant sterols on the hydration and phase behavior of DOPE/DOPC mixtures. Biochim. Biophys. Acta 1239 (1995) 226-238
    • (1995) Biochim. Biophys. Acta , vol.1239 , pp. 226-238
    • Webb, M.S.1    Irving, T.C.2    Steponkus, P.L.3
  • 12
    • 2142699981 scopus 로고    scopus 로고
    • Cytotoxic activity of steroidal glycosides from Solanum plants
    • Ikeda T., Tsumagari H., Honbu T., and Nohara T. Cytotoxic activity of steroidal glycosides from Solanum plants. Biol. Pharm. Bull. 26 (2003) 1198-1201
    • (2003) Biol. Pharm. Bull. , vol.26 , pp. 1198-1201
    • Ikeda, T.1    Tsumagari, H.2    Honbu, T.3    Nohara, T.4
  • 13
    • 27644476269 scopus 로고    scopus 로고
    • Plant secondary metabolism glycosyltransferases: the emerging functional analysis
    • Gachon C.M.M., Langlois-Meurinne M., and Saindrenan P. Plant secondary metabolism glycosyltransferases: the emerging functional analysis. Trends Plant Sci. 10 (2005) 542-549
    • (2005) Trends Plant Sci. , vol.10 , pp. 542-549
    • Gachon, C.M.M.1    Langlois-Meurinne, M.2    Saindrenan, P.3
  • 14
    • 0001154042 scopus 로고
    • Sterol biosynthetic capability of purified membrane fractions from maize coleoptiles
    • Hartmann-Bouillon M.A., and Benveniste P. Sterol biosynthetic capability of purified membrane fractions from maize coleoptiles. Phytochem. 17 (1978) 1037-1043
    • (1978) Phytochem. , vol.17 , pp. 1037-1043
    • Hartmann-Bouillon, M.A.1    Benveniste, P.2
  • 16
    • 19944433661 scopus 로고    scopus 로고
    • Crosstalk and differential response to abiotic and biotic stresses reflected at the transcriptional level of effector genes from secondary metabolism
    • Glombitza S., Dubuis P.H., Thulke O., and Welzl G. Crosstalk and differential response to abiotic and biotic stresses reflected at the transcriptional level of effector genes from secondary metabolism. Plant Mol. Biol. 54 (2004) 817-835
    • (2004) Plant Mol. Biol. , vol.54 , pp. 817-835
    • Glombitza, S.1    Dubuis, P.H.2    Thulke, O.3    Welzl, G.4
  • 18
    • 0030450319 scopus 로고    scopus 로고
    • Preformed antimicrobial compounds and plant defense against fungal attack
    • Osbourn A.E. Preformed antimicrobial compounds and plant defense against fungal attack. Plant Cell 10 (1996) 1821-1831
    • (1996) Plant Cell , vol.10 , pp. 1821-1831
    • Osbourn, A.E.1
  • 19
    • 0027966829 scopus 로고
    • Purification of a membrane-bound UDP-Glucose: sterol β-d-glucosyltransferase based on its solubility in diethyl ether
    • Warnecke D.C., and Heinz E. Purification of a membrane-bound UDP-Glucose: sterol β-d-glucosyltransferase based on its solubility in diethyl ether. Plant Physiol. 105 (1994) 1067-1073
    • (1994) Plant Physiol. , vol.105 , pp. 1067-1073
    • Warnecke, D.C.1    Heinz, E.2
  • 20
    • 0030630190 scopus 로고    scopus 로고
    • UDP-glucose solasodine glucosyltransferase from eggplant (Solanum melongena L.) leaves partial purification and characterization
    • Paczkowski C., Kalinowska M., and Wojciechowski Z.A. UDP-glucose solasodine glucosyltransferase from eggplant (Solanum melongena L.) leaves partial purification and characterization. Acta Biochim. Pol. 44 (1997) 43-53
    • (1997) Acta Biochim. Pol. , vol.44 , pp. 43-53
    • Paczkowski, C.1    Kalinowska, M.2    Wojciechowski, Z.A.3
  • 21
    • 26844582530 scopus 로고    scopus 로고
    • Purification and characterization of UDP-glucose: ginsenoside Rd glucosyltransferase from suspended cells of Panax notoginseng
    • Cai-Jun Y., and Jian-Jiang Z. Purification and characterization of UDP-glucose: ginsenoside Rd glucosyltransferase from suspended cells of Panax notoginseng. Process Biochem. 40 (2005) 3742-3748
    • (2005) Process Biochem. , vol.40 , pp. 3742-3748
    • Cai-Jun, Y.1    Jian-Jiang, Z.2
  • 22
    • 0023146762 scopus 로고
    • The enzymatic mechanism of glucuronidation catalyzed by two purified rat liver steroid UDP-glucuronosyltransferases
    • Falany C.N., Green M.D., and Tephly T.R. The enzymatic mechanism of glucuronidation catalyzed by two purified rat liver steroid UDP-glucuronosyltransferases. J. Biol. Chem. 262 (1987) 1218-1222
    • (1987) J. Biol. Chem. , vol.262 , pp. 1218-1222
    • Falany, C.N.1    Green, M.D.2    Tephly, T.R.3
  • 23
    • 0028693175 scopus 로고
    • Withasteroids, a growing group of naturally occurring steroidal lactones
    • Ray A.B., and Gupta M. Withasteroids, a growing group of naturally occurring steroidal lactones. Fortschr. Chem. Org. Naturst. 63 (1994) 1-106
    • (1994) Fortschr. Chem. Org. Naturst. , vol.63 , pp. 1-106
    • Ray, A.B.1    Gupta, M.2
  • 24
    • 0036593450 scopus 로고    scopus 로고
    • Withanolide derivatives from the roots of Withania somnifera and their neurite outgrowth activities
    • Zhao J., Nakamura N., Hattori M., Kuboyama T., Tohda C., and Komatsu K. Withanolide derivatives from the roots of Withania somnifera and their neurite outgrowth activities. Chem. Pharm. Bull. 50 (2002) 760-765
    • (2002) Chem. Pharm. Bull. , vol.50 , pp. 760-765
    • Zhao, J.1    Nakamura, N.2    Hattori, M.3    Kuboyama, T.4    Tohda, C.5    Komatsu, K.6
  • 25
    • 0034941412 scopus 로고    scopus 로고
    • Structures of withanosides I, II, III, IV, V, VI, and VII, new withanolide glycosides, from the roots of Indian Withania somnifera and inhibitory activity for tachyphylaxis to clonidine in isolated guinea-pig ileum
    • Matsuda H., Murakami T., Kishi A., and Yoshikawa M. Structures of withanosides I, II, III, IV, V, VI, and VII, new withanolide glycosides, from the roots of Indian Withania somnifera and inhibitory activity for tachyphylaxis to clonidine in isolated guinea-pig ileum. Bioorg. Med. Chem. 9 (2001) 1499-1507
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 1499-1507
    • Matsuda, H.1    Murakami, T.2    Kishi, A.3    Yoshikawa, M.4
  • 26
    • 0037415475 scopus 로고    scopus 로고
    • Cyclooxygenase-2 enzyme inhibitory withanolides from Withania somnifera leaves
    • Jayaprakasam B., Muraleetharan, and Nair G. Cyclooxygenase-2 enzyme inhibitory withanolides from Withania somnifera leaves. Tetrahedron 59 (2003) 841-849
    • (2003) Tetrahedron , vol.59 , pp. 841-849
    • Jayaprakasam, B.1    Muraleetharan2    Nair, G.3
  • 27
    • 0031418908 scopus 로고    scopus 로고
    • Antioxidant activity of glycowithanolides from Withania somnifera
    • Bhattacharya S.K., Satyan K.S., and Ghosal S. Antioxidant activity of glycowithanolides from Withania somnifera. Indian J. Exp Biol. 35 (1997) 236-239
    • (1997) Indian J. Exp Biol. , vol.35 , pp. 236-239
    • Bhattacharya, S.K.1    Satyan, K.S.2    Ghosal, S.3
  • 28
    • 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 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0037182233 scopus 로고    scopus 로고
    • Towards manipulation of post-biosynthetic events in secondary metabolism of plant cell cultures
    • Zhang W., Curtin C., and Ranco C. Towards manipulation of post-biosynthetic events in secondary metabolism of plant cell cultures. Enzyme Microb. Technol. 30 (2002) 688-696
    • (2002) Enzyme Microb. Technol. , vol.30 , pp. 688-696
    • Zhang, W.1    Curtin, C.2    Ranco, C.3
  • 30
    • 0034937480 scopus 로고    scopus 로고
    • Glycosyltransferases in secondary plant metabolism: tranquilizers and stimulant controllers
    • Jones P., and Vogt T. Glycosyltransferases in secondary plant metabolism: tranquilizers and stimulant controllers. Planta 213 (2001) 164-174
    • (2001) Planta , vol.213 , pp. 164-174
    • Jones, P.1    Vogt, T.2
  • 31
    • 0018788268 scopus 로고
    • Specificity of sterol-glucosylating enzymes from Sinapis alba and Physarum polycephalum
    • Wojciechowski Z.A., Zimowski J., Zimowski J.G., and Lyznik A. Specificity of sterol-glucosylating enzymes from Sinapis alba and Physarum polycephalum. Biochim. Biophys. Acta 570 (1979) 363-370
    • (1979) Biochim. Biophys. Acta , vol.570 , pp. 363-370
    • Wojciechowski, Z.A.1    Zimowski, J.2    Zimowski, J.G.3    Lyznik, A.4
  • 32
    • 0032146679 scopus 로고    scopus 로고
    • The 3-O-glucosylation of steroidal sapogenins and alkaloids in eggplant (Solanum melongena) evidence for two separate glucosyltransferases
    • Paczkowski C., Kalinowska M., and Wojciechowski Z.A. The 3-O-glucosylation of steroidal sapogenins and alkaloids in eggplant (Solanum melongena) evidence for two separate glucosyltransferases. Phytochem. 48 (1998) 1151-1159
    • (1998) Phytochem. , vol.48 , pp. 1151-1159
    • Paczkowski, C.1    Kalinowska, M.2    Wojciechowski, Z.A.3
  • 33
    • 15544364507 scopus 로고    scopus 로고
    • Genomics-based selection and functional characterization of triterpene glycosyltransferases from the model legume Medicago truncatula
    • Achnine L., Huhman D.V., Farag M.A., Sumner L.W., Blount J.W., and Dixon R.A. Genomics-based selection and functional characterization of triterpene glycosyltransferases from the model legume Medicago truncatula. Plant J. 41 (2005) 875-887
    • (2005) Plant J. , vol.41 , pp. 875-887
    • Achnine, L.1    Huhman, D.V.2    Farag, M.A.3    Sumner, L.W.4    Blount, J.W.5    Dixon, R.A.6
  • 34
    • 33645281589 scopus 로고    scopus 로고
    • Crystal structures of a multifunctional triterpene/flavonoid glycosyltransferase from Medicago trucatula
    • Shao H., He X., Achnine L., Blount J.W., and Dixon R.A. Crystal structures of a multifunctional triterpene/flavonoid glycosyltransferase from Medicago trucatula. Plant Cell 17 (2005) 3141-3154
    • (2005) Plant Cell , vol.17 , pp. 3141-3154
    • Shao, H.1    He, X.2    Achnine, L.3    Blount, J.W.4    Dixon, R.A.5
  • 35
    • 3843126366 scopus 로고    scopus 로고
    • Site-directed mutagenesis and protein 3D-homology modeling suggest a catalytic mechanism for UDP-glucose-dependent betanidin 5-O-glucosyltransferase from Dorotheanthus bellidiformis
    • Hans J., Brandt W., and Vogt T. Site-directed mutagenesis and protein 3D-homology modeling suggest a catalytic mechanism for UDP-glucose-dependent betanidin 5-O-glucosyltransferase from Dorotheanthus bellidiformis. Plant J. 39 (2004) 319-333
    • (2004) Plant J. , vol.39 , pp. 319-333
    • Hans, J.1    Brandt, W.2    Vogt, T.3
  • 37
    • 0025236448 scopus 로고
    • Expression of chimeric c DNA's in cell culture defines a region of UDP glucuronosyltransferase involved in substrate selection
    • Mackenzie P.I. Expression of chimeric c DNA's in cell culture defines a region of UDP glucuronosyltransferase involved in substrate selection. J. Biol. Chem. 265 (1990) 3432-3435
    • (1990) J. Biol. Chem. , vol.265 , pp. 3432-3435
    • Mackenzie, P.I.1
  • 38
    • 0011185761 scopus 로고
    • Regulation by phospholipids and kinetic studies of plant membrane-bound UDP-Glucose sterol β-d-glucosyl transferase
    • Ullmann P., Bouvier-Nave P., and Benveniste P. Regulation by phospholipids and kinetic studies of plant membrane-bound UDP-Glucose sterol β-d-glucosyl transferase. Plant Physiol. 85 (1987) 51-55
    • (1987) Plant Physiol. , vol.85 , pp. 51-55
    • Ullmann, P.1    Bouvier-Nave, P.2    Benveniste, P.3
  • 39
    • 0028331320 scopus 로고
    • Mechanistic studies of uridinediphosphate glucuronosyltransferase
    • Yin H., Bennett G., and Jones J.P. Mechanistic studies of uridinediphosphate glucuronosyltransferase. Chem.-Biol. Interact. 90 (1994) 47-58
    • (1994) Chem.-Biol. Interact. , vol.90 , pp. 47-58
    • Yin, H.1    Bennett, G.2    Jones, J.P.3
  • 40
    • 0025900605 scopus 로고
    • Partial purification, properties and kinetic studies of UDP-glucose:p-hydroxybenzoate glucosyltransferase from cell cultures of Lithospermum erythorihizon
    • Bechthold A., Berger U., and Heide L. Partial purification, properties and kinetic studies of UDP-glucose:p-hydroxybenzoate glucosyltransferase from cell cultures of Lithospermum erythorihizon. Arch. Biochem. Biophys. 288 (1991) 39-47
    • (1991) Arch. Biochem. Biophys. , vol.288 , pp. 39-47
    • Bechthold, A.1    Berger, U.2    Heide, L.3
  • 41
    • 0038826955 scopus 로고    scopus 로고
    • Inducers of plant systemic acquired resistance regulate NPR1 function through redox changes
    • Mou Z., Fan W., and Dong X. Inducers of plant systemic acquired resistance regulate NPR1 function through redox changes. Cell 113 (2003) 935-944
    • (2003) Cell , vol.113 , pp. 935-944
    • Mou, Z.1    Fan, W.2    Dong, X.3
  • 42
    • 0031079999 scopus 로고    scopus 로고
    • Cloning and expression of solanidine UDP-glucose glucosyltransferase from potato
    • Moehs C.P., Allen P.V., Friedman M., and Belknap W.R. Cloning and expression of solanidine UDP-glucose glucosyltransferase from potato. Plant J. 11 (1997) 227-236
    • (1997) Plant J. , vol.11 , pp. 227-236
    • Moehs, C.P.1    Allen, P.V.2    Friedman, M.3    Belknap, W.R.4
  • 44
    • 0024430427 scopus 로고
    • Expression of UDP-glucose poriferasterol glucosyltransferase in the process of differentiation of a true slime mold, Physarum polycephalum
    • Murakami-Murofushi K., and Ohta J. Expression of UDP-glucose poriferasterol glucosyltransferase in the process of differentiation of a true slime mold, Physarum polycephalum. Biochim. Biophys. Acta 992 (1989) 412-415
    • (1989) Biochim. Biophys. Acta , vol.992 , pp. 412-415
    • Murakami-Murofushi, K.1    Ohta, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.