메뉴 건너뛰기




Volumn 205, Issue 3, 1998, Pages 407-413

4-Hydroxybenzoate 3-geranyltransferase from Lithospermum erythrorhizon: Purification of a plant membrane-bound prenyltransferase

Author keywords

Geranyltransferase; Lithospermum; Methyl jasmonate; Prenyltransferase; Shikonin

Indexed keywords

4 HYDROXYBENZOATE 3 GERANYLTRANSFERASE; CHROMATOGRAPHY; DIMETHYLALLYLTRANSFERASE; ENZYME KINETICS; ENZYME PURIFICATION; PHYTOALEXIN; SHIKONIN;

EID: 2142835098     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004250050337     Document Type: Article
Times cited : (44)

References (35)
  • 1
    • 0026731820 scopus 로고
    • COQ2 is a candidate for the structural gene encoding para-hydroxybenzoate:polyprenyltransferase
    • Ashby MN, Kutsunai SY, Ackerman S, Tzagoloff A, Edwards PA (1992) COQ2 is a candidate for the structural gene encoding para-hydroxybenzoate:polyprenyltransferase. J Biol Chem 267: 4128-1136
    • (1992) J Biol Chem , vol.267 , pp. 4128-11136
    • Ashby, M.N.1    Kutsunai, S.Y.2    Ackerman, S.3    Tzagoloff, A.4    Edwards, P.A.5
  • 2
    • 0001357283 scopus 로고
    • Dimethylallyl-pyrophosphate: 3,9-dihydroxypterocarpan 10-dimethylallyl transferase from Phaseolus vulgaris
    • Biggs DR, Welle R, Visser FR, Grisebach H (1987) Dimethylallyl-pyrophosphate: 3,9-dihydroxypterocarpan 10-dimethylallyl transferase from Phaseolus vulgaris. FEBS Lett 220: 223-226
    • (1987) FEBS Lett , vol.220 , pp. 223-226
    • Biggs, D.R.1    Welle, R.2    Visser, F.R.3    Grisebach, H.4
  • 3
    • 0001557214 scopus 로고
    • Intracellular localization of prenyltransferases of isoflavonoid phytoalexin biosynthesis in bean and soybean
    • Biggs DR, Welle R, Grisebach H (1990) Intracellular localization of prenyltransferases of isoflavonoid phytoalexin biosynthesis in bean and soybean. Planta 181: 244-248
    • (1990) Planta , vol.181 , pp. 244-248
    • Biggs, D.R.1    Welle, R.2    Grisebach, H.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0001233898 scopus 로고
    • Chemical syntheses of substrates of sterol biosynthesis
    • Cornforth RH, Popjak G (1969) Chemical syntheses of substrates of sterol biosynthesis. Methods Enzymol 15: 359-390
    • (1969) Methods Enzymol , vol.15 , pp. 359-390
    • Cornforth, R.H.1    Popjak, G.2
  • 6
    • 0004962601 scopus 로고
    • Uäber die Anatomie von Radix Lithospermi
    • Fujita N, Yosida Y (1937) Uäber die Anatomie von Radix Lithospermi. Yakugaku Zasshi 57: 368-391
    • (1937) Yakugaku Zasshi , vol.57 , pp. 368-391
    • Fujita, N.1    Yosida, Y.2
  • 7
    • 0002714732 scopus 로고
    • Production of shikonin derivatives by cell suspension cultures of Lithospermum erythrorhizon. I. Effects of nitrogen sources on the production of shikonin derivatives
    • Fujita Y, Hara Y, Ogino T, Suga C (1981a) Production of shikonin derivatives by cell suspension cultures of Lithospermum erythrorhizon. I. Effects of nitrogen sources on the production of shikonin derivatives. Plant Cell Rep 1: 59-60
    • (1981) Plant Cell Rep , vol.1 , pp. 59-60
    • Fujita, Y.1    Hara, Y.2    Ogino, T.3    Suga, C.4
  • 8
    • 0002714734 scopus 로고
    • Production of shikonin derivatives by cell suspension cultures of Lithospermum erythrorhizon. II A new medium for the production of shikonin derivatives
    • Fujita Y, Hara Y, Suga C, Morimoto T (1981b) Production of shikonin derivatives by cell suspension cultures of Lithospermum erythrorhizon. II A new medium for the production of shikonin derivatives. Plant Cell Rep 1: 61-63
    • (1981) Plant Cell Rep , vol.1 , pp. 61-63
    • Fujita, Y.1    Hara, Y.2    Suga, C.3    Morimoto, T.4
  • 9
    • 0030019335 scopus 로고    scopus 로고
    • Inhibition and regulation of shikonin biosynthesis in suspension cultures of Lithospermum
    • Gaisser S, Heide L (1996) Inhibition and regulation of shikonin biosynthesis in suspension cultures of Lithospermum. Phytochemistry 41: 1065-1072
    • (1996) Phytochemistry , vol.41 , pp. 1065-1072
    • Gaisser, S.1    Heide, L.2
  • 10
    • 0026520785 scopus 로고
    • Jasmonic acid is a signal transducer in elicitor-induced plant cell cultures
    • Gundlach H, Muäller MJ, Kutchan TM, Zenk MH (1992) Jasmonic acid is a signal transducer in elicitor-induced plant cell cultures Proc Natl Acad Sci USA 89: 2389-2393
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2389-2393
    • Gundlach, H.1    Muäller, M.J.2    Kutchan, T.M.3    Zenk, M.H.4
  • 11
    • 0025140399 scopus 로고
    • Induction of two prenyltransferases for the accumulation of coumarin phytoalexins in elicitor-treated Ammi majus cell suspension cultures
    • Hamerski D, Schmitt D, Matern U (1990) Induction of two prenyltransferases for the accumulation of coumarin phytoalexins in elicitor-treated Ammi majus cell suspension cultures. Phytochemistry 29: 1131-1135
    • (1990) Phytochemistry , vol.29 , pp. 1131-1135
    • Hamerski, D.1    Schmitt, D.2    Matern, U.3
  • 12
    • 0000083514 scopus 로고
    • Geranylpyrophosphate:p-hydroxybenzoate geranyltransferase in extracts of Lithospermum erythrorhizon cell cultures
    • Heide L, Tabata M (1987) Geranylpyrophosphate:p-hydroxybenzoate geranyltransferase in extracts of Lithospermum erythrorhizon cell cultures. Phytochemistry 26: 1651-1655
    • (1987) Phytochemistry , vol.26 , pp. 1651-1655
    • Heide, L.1    Tabata, M.2
  • 13
    • 0001051044 scopus 로고
    • Incorporation of shikimic acid into p-hydroxybenzoic acid in Lithospermum erythrorhizon cell cultures
    • Heide L, Floss HG, Tabata M (1989a) Incorporation of shikimic acid into p-hydroxybenzoic acid in Lithospermum erythrorhizon cell cultures. Phytochemistry 28: 2643-2645
    • (1989) Phytochemistry , vol.28 , pp. 2643-2645
    • Heide, L.1    Floss, H.G.2    Tabata, M.3
  • 14
    • 0001051043 scopus 로고
    • Enzymatic regulation of shikonin biosynthesis in Lithospermum erythrorhizon cell cultures
    • Heide L, Nishioka N, Fukui H, Tabata M (1989b) Enzymatic regulation of shikonin biosynthesis in Lithospermum erythrorhizon cell cultures. Phytochemistry 28: 1873-1877
    • (1989) Phytochemistry , vol.28 , pp. 1873-1877
    • Heide, L.1    Nishioka, N.2    Fukui, H.3    Tabata, M.4
  • 15
    • 0025252193 scopus 로고
    • Solubilization of native membrane proteins
    • Hjelmeland LM (1990) Solubilization of native membrane proteins. Methods Enzymol 182: 253-276
    • (1990) Methods Enzymol , vol.182 , pp. 253-276
    • Hjelmeland, L.M.1
  • 17
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H, Burk D (1934) The determination of enzyme dissociation constants. J Am Chem Soc 56: 658-666
    • (1934) J Am Chem Soc , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 18
    • 84982378007 scopus 로고
    • Organic growth factor requirements of tobacco tissue cultures
    • Linsmaier ML, Skoog F (1965) Organic growth factor requirements of tobacco tissue cultures. Physiol Plant 18: 100-127
    • (1965) Physiol Plant , vol.18 , pp. 100-127
    • Linsmaier, M.L.1    Skoog, F.2
  • 19
    • 0027951993 scopus 로고
    • Biosynthesis of p-hydroxybenzoate from p-coumarate and p-coumaroyl-coenzyme A in cell-free extracts of Lithospermum erythrorhizon cell cultures
    • Loäscher R. Heide L (1994) Biosynthesis of p-hydroxybenzoate from p-coumarate and p-coumaroyl-coenzyme A in cell-free extracts of Lithospermum erythrorhizon cell cultures. Plant Physiol 106: 271-279
    • (1994) Plant Physiol , vol.106 , pp. 271-279
    • Loäscher, R.1    Heide, L.2
  • 20
    • 0001431626 scopus 로고
    • Synthesis of 1.3-dihydroxy-N-methyl-acridone and its conversion to rutacridone by cell-free extracts of Ruta graveolens cell cultures
    • Maier W, Baumert A, Schumann B, Furukawa H, Groäger D (1993) Synthesis of 1.3-dihydroxy-N-methyl-acridone and its conversion to rutacridone by cell-free extracts of Ruta graveolens cell cultures. Phytochemistry 32: 691-698
    • (1993) Phytochemistry , vol.32 , pp. 691-698
    • Maier, W.1    Baumert, A.2    Schumann, B.3    Furukawa, H.4    Groäger, D.5
  • 21
    • 0028180730 scopus 로고
    • Characterization of polyprenyldiphosphate:4-hydroxybenzoate polyprenyltransferase from Escherichia coli
    • Melzer M, Heide L (1994) Characterization of polyprenyldiphosphate:4-hydroxybenzoate polyprenyltransferase from Escherichia coli. Biochim Biophys Acta 1212: 93-102
    • (1994) Biochim Biophys Acta , vol.1212 , pp. 93-102
    • Melzer, M.1    Heide, L.2
  • 22
    • 0030299216 scopus 로고    scopus 로고
    • Occurrence of phytoalexins and phenolic compounds in endomycorrhizal interactions, and their potential role in biological control
    • Morandi D (1996) Occurrence of phytoalexins and phenolic compounds in endomycorrhizal interactions, and their potential role in biological control. Plant Soil 185: 241-251
    • (1996) Plant Soil , vol.185 , pp. 241-251
    • Morandi, D.1
  • 23
    • 24444463360 scopus 로고
    • Uäber die Verbreitung des Alkannins bei den Borragineen und sein Auftreten in der Pflanze
    • Pulitzer G (1915) Uäber die Verbreitung des Alkannins bei den Borragineen und sein Auftreten in der Pflanze. Oästerr Bot Zeit 7/8: 177-190
    • (1915) Oästerr Bot Zeit , vol.7-8 , pp. 177-190
    • Pulitzer, G.1
  • 24
    • 0018399218 scopus 로고
    • Biosynthesis of antifungal isoflavonoids in Lupinus albus. Enzymatic prenylation of genistein and 2′-hydroxygenistein
    • Schroäder G, Zaähringer U, Heller W, Ebel J, Grisebach H (1979) Biosynthesis of antifungal isoflavonoids in Lupinus albus. Enzymatic prenylation of genistein and 2′-hydroxygenistein. Arch Biochem Biophys 194: 635-636
    • (1979) Arch Biochem Biophys , vol.194 , pp. 635-636
    • Schroäder, G.1    Zaähringer, U.2    Heller, W.3    Ebel, J.4    Grisebach, H.5
  • 25
    • 0027110704 scopus 로고
    • Ubiquinone biosynthesis. Cloning of the genes coding for chorismate pyruvate-lyase and 4-hydroxybenzoate octaprenyl transferase from Escherichia coli
    • Siebert M, Bechthold A. Melzer M, May U, Berger U, Schroäder G, Schroäder J, Severin K, Heide L (1992) Ubiquinone biosynthesis. Cloning of the genes coding for chorismate pyruvate-lyase and 4-hydroxybenzoate octaprenyl transferase from Escherichia coli. FEBS Lett 307: 347-350
    • (1992) FEBS Lett , vol.307 , pp. 347-350
    • Siebert, M.1    Bechthold, A.2    Melzer, M.3    May, U.4    Berger, U.5    Schroäder, G.6    Schroäder, J.7    Severin, K.8    Heide, L.9
  • 26
    • 0029141329 scopus 로고
    • Intracellular localization of geranylpyrophosphate synthase from cell cultures of Lithospermum erythrorhizon
    • Sommer S, Severin K, Camara B, Heide L (1995) Intracellular localization of geranylpyrophosphate synthase from cell cultures of Lithospermum erythrorhizon. Phytochemistry 38: 623-627
    • (1995) Phytochemistry , vol.38 , pp. 623-627
    • Sommer, S.1    Severin, K.2    Camara, B.3    Heide, L.4
  • 27
    • 0002439098 scopus 로고
    • Production of shikonin by plant cell cultures
    • Day P, Zaitlin M, Hollaender A (eds). Academic Press, Orlando
    • Tabata M, Fujita Y (1985) Production of shikonin by plant cell cultures. In: Day P, Zaitlin M, Hollaender A (eds) Biotechnology in plant science. Academic Press, Orlando, pp 207-218
    • (1985) Biotechnology in Plant Science , pp. 207-218
    • Tabata, M.1    Fujita, Y.2
  • 28
    • 0029135787 scopus 로고
    • Prenylated isoflavonoids-an update
    • Tahara S, Ibrahim RK (1995) Prenylated isoflavonoids-an update. Phytochemistry 38: 1073-1094
    • (1995) Phytochemistry , vol.38 , pp. 1073-1094
    • Tahara, S.1    Ibrahim, R.K.2
  • 30
    • 0027141196 scopus 로고
    • Effects of oligogalacturonides on biosynthesis of shikonin in Lithospermum cell cultures
    • Tani M, Takeda K, Yazaki K, Tabata M (1993) Effects of oligogalacturonides on biosynthesis of shikonin in Lithospermum cell cultures. Phytochemistry 34: 1285-1290
    • (1993) Phytochemistry , vol.34 , pp. 1285-1290
    • Tani, M.1    Takeda, K.2    Yazaki, K.3    Tabata, M.4
  • 31
    • 0025233343 scopus 로고
    • Purification of membrane proteins
    • Thomas CT, McNamee MG (1990) Purification of membrane proteins. Methods Enzymol 182: 499-520
    • (1990) Methods Enzymol , vol.182 , pp. 499-520
    • Thomas, C.T.1    McNamee, M.G.2
  • 32
    • 0000597314 scopus 로고
    • Intracellular localization and secretion of naphthoquinone pigments in cell cultures of Lithospermum erythrorhizon
    • Tsukada M, Tabata M (1984) Intracellular localization and secretion of naphthoquinone pigments in cell cultures of Lithospermum erythrorhizon. Planta Med 50: 338-340
    • (1984) Planta Med , vol.50 , pp. 338-340
    • Tsukada, M.1    Tabata, M.2
  • 33
    • 0001233414 scopus 로고
    • Properties and solubilization of the prenyltransferase of isoflavonoid phytoalexin biosynthesis in soybean
    • Welle R, Grisebach H (1991) Properties and solubilization of the prenyltransferase of isoflavonoid phytoalexin biosynthesis in soybean. Phytochemistry 30: 479-484
    • (1991) Phytochemistry , vol.30 , pp. 479-484
    • Welle, R.1    Grisebach, H.2
  • 34
    • 0000247541 scopus 로고
    • Intracellular localization of p-hydroxybenzoate geranyltransferase, a key enzyme involved in shikonin biosynthesis
    • Yamaga Y, Nakanishi K, Fukui H, Tabata M (1993) Intracellular localization of p-hydroxybenzoate geranyltransferase, a key enzyme involved in shikonin biosynthesis. Phytochemistry 32: 633-636
    • (1993) Phytochemistry , vol.32 , pp. 633-636
    • Yamaga, Y.1    Nakanishi, K.2    Fukui, H.3    Tabata, M.4
  • 35
    • 0029917011 scopus 로고    scopus 로고
    • Linearization of the Bradford protein assay increases its sensitivity: Theoretical and experimental studies
    • Zor T, Selinger Z (1996) Linearization of the Bradford protein assay increases its sensitivity: theoretical and experimental studies. Anal Biochem 236: 302-308
    • (1996) Anal Biochem , vol.236 , pp. 302-308
    • Zor, T.1    Selinger, Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.