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Volumn 249, Issue 1, 1997, Pages 161-170

Purification and characterization of two isoforms of isopentenyl-diphosphate isomerase from elicitor-treated Cinchona robusta cells

Author keywords

Anthraquinone; Cinchona; Elicitation; Isopentenyl diphosphate isomerase; Phytoalexin

Indexed keywords

ISOENZYME; ISOMERASE;

EID: 0030861518     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-1-00161.x     Document Type: Article
Times cited : (34)

References (47)
  • 1
    • 0028156656 scopus 로고
    • Light-stimulated carotenoid biosynthesis during transformation of maize etioplasts is regulated by increased activity of isopentenyl pyrophosphate isomerase
    • Albrecht, M. & Sandmann, G. (1994) Light-stimulated carotenoid biosynthesis during transformation of maize etioplasts is regulated by increased activity of isopentenyl pyrophosphate isomerase, Plant Physiol. (Bethesda) 105, 529-534.
    • (1994) Plant Physiol. (Bethesda) , vol.105 , pp. 529-534
    • Albrecht, M.1    Sandmann, G.2
  • 2
    • 0024789309 scopus 로고
    • Isopentenyl diphosphate:dimethylallyl diphosphate isomerase. An improved purification of the enzyme and isolation of the gene from Saccharomyces cerevisiae
    • Anderson, M. S., Muehlbacher, M. Street, I. P., Proffitt, J. & Poulter, C. D. (1989) Isopentenyl diphosphate:dimethylallyl diphosphate isomerase. An improved purification of the enzyme and isolation of the gene from Saccharomyces cerevisiae, J. Biol. Chem. 264, 19169-19175.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19169-19175
    • Anderson, M.S.1    Muehlbacher, M.2    Street, I.P.3    Proffitt, J.4    Poulter, C.D.5
  • 5
    • 0029315124 scopus 로고
    • Nucleotide sequence of a Clarkia breweri cDNA clone of Ipi1, a gene encoding isopentenyl diphosphate isomerase
    • Blanc, V. & Pichersky, E. (1995) Nucleotide sequence of a Clarkia breweri cDNA clone of Ipi1, a gene encoding isopentenyl diphosphate isomerase, Plant Physiol. (Bethesda) 108, 855-856.
    • (1995) Plant Physiol. (Bethesda) , vol.108 , pp. 855-856
    • Blanc, V.1    Pichersky, E.2
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0022761644 scopus 로고
    • Isopentenyl pyrophosphate isomerase:dimethylallyl pyrophosphate isomerase: Isolation from Claviceps sp. SD 58 and comparision to the mammalian enzyme
    • Bruenger, E., Chayet, L. & Rilling, H. C. (1986) Isopentenyl pyrophosphate isomerase:dimethylallyl pyrophosphate isomerase: isolation from Claviceps sp. SD 58 and comparision to the mammalian enzyme, Arch. Biochem. Biophys. 248, 620-625.
    • (1986) Arch. Biochem. Biophys. , vol.248 , pp. 620-625
    • Bruenger, E.1    Chayet, L.2    Rilling, H.C.3
  • 8
    • 0011885531 scopus 로고
    • Enzymology of isoprenoid biosynthesis and expression of plastid and nuclear genes during chromoplast differentiation in pepper fruits (Capsicum annuum)
    • (Boyer, C. D., Shannon, J. C. & Hardison, R. C, eds) American Society of Plant Physiologists
    • Camara, B., Bousquet, J., Cheniclet, C., Carde, J. P., Kuntz, M., Evrard, J. L. & Weil, J. H. (1989) Enzymology of isoprenoid biosynthesis and expression of plastid and nuclear genes during chromoplast differentiation in pepper fruits (Capsicum annuum), in Physiology, biochemistry and genetics of nongreen plastids (Boyer, C. D., Shannon, J. C. & Hardison, R. C, eds) pp. 141-156, American Society of Plant Physiologists.
    • (1989) Physiology, Biochemistry and Genetics of Nongreen Plastids , pp. 141-156
    • Camara, B.1    Bousquet, J.2    Cheniclet, C.3    Carde, J.P.4    Kuntz, M.5    Evrard, J.L.6    Weil, J.H.7
  • 9
    • 0021949079 scopus 로고
    • Monoterpene and sesquiterpene cyclases
    • Croteau, R. & Cane, D. E. (1985) Monoterpene and sesquiterpene cyclases, Methods Enzymol. 110, 383-495.
    • (1985) Methods Enzymol. , vol.110 , pp. 383-495
    • Croteau, R.1    Cane, D.E.2
  • 10
    • 0021977216 scopus 로고
    • Synthesis of allylic and homoallylic isoprenoids pyrophosphates
    • Davisson, V. J., Woodside, A. B. & Poulter, C. D. (1985) Synthesis of allylic and homoallylic isoprenoids pyrophosphates, Methods Enzymol. 110, 130-144.
    • (1985) Methods Enzymol. , vol.110 , pp. 130-144
    • Davisson, V.J.1    Woodside, A.B.2    Poulter, C.D.3
  • 11
    • 0001042248 scopus 로고
    • Purification of isopentenyl pyrophosphate isomerase and geranylgeranyl pyrophosphate synthase from Capsicum chromoplasts by affinity chromatography
    • Dogbo, O. & Camara, B. (1987) Purification of isopentenyl pyrophosphate isomerase and geranylgeranyl pyrophosphate synthase from Capsicum chromoplasts by affinity chromatography, Biochim. Biophys. Acta 920, 140-148.
    • (1987) Biochim. Biophys. Acta , vol.920 , pp. 140-148
    • Dogbo, O.1    Camara, B.2
  • 12
    • 0343493111 scopus 로고
    • The photoregulation of carotenoid biosynthesis in Aspergillus giganteus mut. alba
    • El-Jack, M., Mackenzie, A. & Bramley, P. M. (1988) The photoregulation of carotenoid biosynthesis in Aspergillus giganteus mut. alba, Planta (Heidelb.) 174, 59-66.
    • (1988) Planta (Heidelb.) , vol.174 , pp. 59-66
    • El-Jack, M.1    Mackenzie, A.2    Bramley, P.M.3
  • 13
    • 0022542607 scopus 로고
    • Isoprenoid synthesis in Escherichia coli. Separation and partial purification of four enzymes involved in the synthesis
    • Fujisaki, S., Nishino, T. & Katsuki, H. (1986) Isoprenoid synthesis in Escherichia coli. Separation and partial purification of four enzymes involved in the synthesis, J. Biochem. (Tokyo) 99, 1327-1337.
    • (1986) J. Biochem. (Tokyo) , vol.99 , pp. 1327-1337
    • Fujisaki, S.1    Nishino, T.2    Katsuki, H.3
  • 14
    • 0003038709 scopus 로고
    • Regulation of monoterpene biosynthesis in higher plants
    • (Towers, G. H. N. & Stafford, H., eds) Plenum Press, New York
    • Gershenzon, J. & Croteau, R. (1990) Regulation of monoterpene biosynthesis in higher plants, in Biochemistry of the mevalonic acid pathway to terpenoids (Towers, G. H. N. & Stafford, H., eds) pp. 99-160, Plenum Press, New York.
    • (1990) Biochemistry of the Mevalonic Acid Pathway to Terpenoids , pp. 99-160
    • Gershenzon, J.1    Croteau, R.2
  • 15
    • 77956841955 scopus 로고
    • Control of isoprenoid biosynthesis in higher plants
    • Gray, J. C. (1987) Control of isoprenoid biosynthesis in higher plants, Adv. Bot. Res. 14, 25-90.
    • (1987) Adv. Bot. Res. , vol.14 , pp. 25-90
    • Gray, J.C.1
  • 17
    • 0038097483 scopus 로고
    • Enzyme activities in extracts of anthraquinone-containing cells of Galium mollugo
    • Heide, L. & Leistner, E. (1983) Enzyme activities in extracts of anthraquinone-containing cells of Galium mollugo, Phytochemistry (Oxf.) 22, 659-662.
    • (1983) Phytochemistry (Oxf.) , vol.22 , pp. 659-662
    • Heide, L.1    Leistner, E.2
  • 18
    • 0014103819 scopus 로고
    • The purification of 3,3,-dimethylallyl- And geranyltransferase and isopentenyl pyrophosphate isomerase from liver
    • Holloway, P. W. & Popjak, G. (1967) The purification of 3,3,-dimethylallyl- and geranyltransferase and isopentenyl pyrophosphate isomerase from liver, Biochem. J. 104, 57-70.
    • (1967) Biochem. J. , vol.104 , pp. 57-70
    • Holloway, P.W.1    Popjak, G.2
  • 19
    • 0025169595 scopus 로고
    • Purification and characterization of farnesyl pyrophosphate synthase from Capsicum annuum
    • Hugueney, P. & Camara, B. (1990) Purification and characterization of farnesyl pyrophosphate synthase from Capsicum annuum, FEBS Lett. 273, 235-238.
    • (1990) FEBS Lett. , vol.273 , pp. 235-238
    • Hugueney, P.1    Camara, B.2
  • 22
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose
    • Kyhse-Anderson, J. (1984) Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose, J. Biochem. Biophys. Methods 10, 203-209.
    • (1984) J. Biochem. Biophys. Methods , vol.10 , pp. 203-209
    • Kyhse-Anderson, J.1
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0001592259 scopus 로고
    • The isopentenyl diphosphate isomerase and its relation to the phytoene synthase complex in daffodil chromoplasts
    • Lützow, M. & Beyer, P. (1988) The isopentenyl diphosphate isomerase and its relation to the phytoene synthase complex in daffodil chromoplasts, Biochim. Biophys. Acta 959, 118-126.
    • (1988) Biochim. Biophys. Acta , vol.959 , pp. 118-126
    • Lützow, M.1    Beyer, P.2
  • 25
    • 0017579190 scopus 로고
    • The diversion of dimethylallyl pyrophosphate from polyisoprenoid to cyclopiazonic acid biosynthesis in Penicillium cyclopium Westling
    • McGrath, M., Nourse, P. N., Neethling, D. C. & Ferreira, N. P. (1977) The diversion of dimethylallyl pyrophosphate from polyisoprenoid to cyclopiazonic acid biosynthesis in Penicillium cyclopium Westling, Bioorg. Chem. 6, 53-69.
    • (1977) Bioorg. Chem. , vol.6 , pp. 53-69
    • McGrath, M.1    Nourse, P.N.2    Neethling, D.C.3    Ferreira, N.P.4
  • 26
    • 0024293191 scopus 로고
    • Isopentenyl-diphosphate isomerase: Inactivation of the enzyme with active-site-directed irreversible inhibitors and transition-state analogues
    • Muehlbacher, M. & Poulter, C. D. (1988) Isopentenyl-diphosphate isomerase: inactivation of the enzyme with active-site-directed irreversible inhibitors and transition-state analogues, Biochemistry 27, 7315-7328.
    • (1988) Biochemistry , vol.27 , pp. 7315-7328
    • Muehlbacher, M.1    Poulter, C.D.2
  • 27
    • 0014316478 scopus 로고
    • The purification of prenyltransferases and isopentenyl pyrophosphate isomerase of pumpkin fruit and some of their properties
    • Ogura, K., Nishino, T. & Seto, S. (1968) The purification of prenyltransferases and isopentenyl pyrophosphate isomerase of pumpkin fruit and some of their properties, J. Biochem. (Tokyo) 64, 197-203.
    • (1968) J. Biochem. (Tokyo) , vol.64 , pp. 197-203
    • Ogura, K.1    Nishino, T.2    Seto, S.3
  • 28
    • 0014542257 scopus 로고
    • Inhibitory effect of substrate analogs on isopentenyl pyrophosphate isomerase and prenyltransferase
    • Ogura, K., Koyama, T., Shibuya, T., Nishino, T. & Seto, S. (1969) Inhibitory effect of substrate analogs on isopentenyl pyrophosphate isomerase and prenyltransferase, J. Biochem. (Tokyo) 66, 117-118.
    • (1969) J. Biochem. (Tokyo) , vol.66 , pp. 117-118
    • Ogura, K.1    Koyama, T.2    Shibuya, T.3    Nishino, T.4    Seto, S.5
  • 29
    • 9844245938 scopus 로고
    • Two isopentenyl pyrophosphate isomerases from pumpkin fruit
    • Ogura, K., Nishino, T., Koyama, T. & Seto, S. (1971) Two isopentenyl pyrophosphate isomerases from pumpkin fruit, Phytochemistry (Oxf.) 10, 779-781.
    • (1971) Phytochemistry (Oxf.) , vol.10 , pp. 779-781
    • Ogura, K.1    Nishino, T.2    Koyama, T.3    Seto, S.4
  • 30
    • 0023774901 scopus 로고
    • EZ-FIT: A practical curve-fitting microcomputer program for the analysis of enzyme kinetic data on IBM-PC compatible computers
    • Perrella, F. W. (1988) EZ-FIT: a practical curve-fitting microcomputer program for the analysis of enzyme kinetic data on IBM-PC compatible computers, Anal. Biochem. 174, 437-447.
    • (1988) Anal. Biochem. , vol.174 , pp. 437-447
    • Perrella, F.W.1
  • 31
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson, G. L. (1977) A simplification of the protein assay method of Lowry et al. which is more generally applicable, Anal. Biochem. 83, 346-356.
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 32
    • 0000680126 scopus 로고
    • Prenyltransferase and isomerase
    • (Porter, J. W. & Spurgeon, S. L., eds) John Wiley, New York
    • Poulter, C. D. & Rilling, H. C. (1981) Prenyltransferase and isomerase, in Biosynthesis of isoprenoid compounds (Porter, J. W. & Spurgeon, S. L., eds) pp. 160-224, John Wiley, New York.
    • (1981) Biosynthesis of Isoprenoid Compounds , pp. 160-224
    • Poulter, C.D.1    Rilling, H.C.2
  • 34
    • 0030722452 scopus 로고    scopus 로고
    • Elicitor-mediated induction of anthraquinone biosynthesis and regulation of isopentenyl diphosphate isomerase and farnesyl diphosphate synthase activities in cell suspension cultures of C. robusta
    • in the press
    • Ramos-Valdivia, A. C., van der Heijden, R. & Verpoorte, R. (1997a) Elicitor-mediated induction of anthraquinone biosynthesis and regulation of isopentenyl diphosphate isomerase and farnesyl diphosphate synthase activities in cell suspension cultures of C. robusta, Planta (Heidelb.), in the press.
    • (1997) Planta (Heidelb.)
    • Ramos-Valdivia, A.C.1    Van Der Heijden, R.2    Verpoorte, R.3
  • 35
    • 0031434083 scopus 로고    scopus 로고
    • Isopentenyl diphosphate isomerase: A core enzyme in isoprenoid biosynthesis. A review of its biochemistry and function
    • in the press
    • Ramos-Valdivia, A. C., van der Heijden, R. & Verpoorte, R. (1997b) Isopentenyl diphosphate isomerase: a core enzyme in isoprenoid biosynthesis. A review of its biochemistry and function, Nat. Prod. Rep., in the press.
    • (1997) Nat. Prod. Rep.
    • Ramos-Valdivia, A.C.1    Van Der Heijden, R.2    Verpoorte, R.3
  • 36
    • 0023055756 scopus 로고
    • Mechanism of action of isopentenyl pyrophosphate isomerase: Evidence for a carbonium ion intermediate
    • Reardon, J. E. & Abeles, R. H. (1986) Mechanism of action of isopentenyl pyrophosphate isomerase: evidence for a carbonium ion intermediate, Biochemistry 25, 5609-5616.
    • (1986) Biochemistry , vol.25 , pp. 5609-5616
    • Reardon, J.E.1    Abeles, R.H.2
  • 37
    • 0020818335 scopus 로고
    • Multiple forms of isopentenyl pyrophosphate isomerase of avian liver
    • Sagami, H. & Ogura, K. (1983) Multiple forms of isopentenyl pyrophosphate isomerase of avian liver, J. Biochem. (Tokyo) 94, 975-979.
    • (1983) J. Biochem. (Tokyo) , vol.94 , pp. 975-979
    • Sagami, H.1    Ogura, K.2
  • 38
    • 0021894248 scopus 로고
    • Isopentenyl diphosphate isomerase
    • Satterwhite, D. M. (1985) Isopentenyl diphosphate isomerase, Methods Enzymol. 110, 92-99.
    • (1985) Methods Enzymol. , vol.110 , pp. 92-99
    • Satterwhite, D.M.1
  • 40
    • 9844225660 scopus 로고
    • The partial purification, properties and mechanism of action of pig liver isopentenyl diphosphate isomerase
    • Shah, D. H., Cleland, W. W. & Porter, J. W. (1965) The partial purification, properties and mechanism of action of pig liver isopentenyl diphosphate isomerase, J. Biol. Chem. 240, 1946-1956.
    • (1965) J. Biol. Chem. , vol.240 , pp. 1946-1956
    • Shah, D.H.1    Cleland, W.W.2    Porter, J.W.3
  • 41
    • 0021267177 scopus 로고
    • Identification, developmental regulation, and response to heat shock of two antigenically related forms of a major nuclear envelope protein in Drosophila embryos: Application of an improved method for affinity purification of antibodies using polypeptides immobilized on nitrocellulose blots
    • Smith, D. E. & Fisher, P. A. (1984) Identification, developmental regulation, and response to heat shock of two antigenically related forms of a major nuclear envelope protein in Drosophila embryos: application of an improved method for affinity purification of antibodies using polypeptides immobilized on nitrocellulose blots, J. Cell. Biol. 99, 20-28.
    • (1984) J. Cell. Biol. , vol.99 , pp. 20-28
    • Smith, D.E.1    Fisher, P.A.2
  • 42
    • 0021430314 scopus 로고
    • The isopentenyl pyrophosphate isomerase and prenyltranferase from tomato fruit plastids
    • Spurgeon, S. L., Sathyamoorthy, N. & Porter, J. W. (1984) The isopentenyl pyrophosphate isomerase and prenyltranferase from tomato fruit plastids, Arch. Biochem. Biophys. 230, 446-454.
    • (1984) Arch. Biochem. Biophys. , vol.230 , pp. 446-454
    • Spurgeon, S.L.1    Sathyamoorthy, N.2    Porter, J.W.3
  • 43
    • 0025025784 scopus 로고
    • Isopentenyl diphosphate:dimethylallyl diphosphate isomerase: Construction of a high-level heterologous expression system for the gene from Saccharomyces cerevisiae and identification of an active-site nucleophile
    • Street, I. P. & Poulter, C. D. (1990) Isopentenyl diphosphate:dimethylallyl diphosphate isomerase: construction of a high-level heterologous expression system for the gene from Saccharomyces cerevisiae and identification of an active-site nucleophile, Biochemistry 29, 7531-7538.
    • (1990) Biochemistry , vol.29 , pp. 7531-7538
    • Street, I.P.1    Poulter, C.D.2
  • 44
    • 0001357263 scopus 로고
    • Geranyl diphosphate synthase in leaves of Pelargonium roseum
    • Suga, T. & Endo, T. (1991) Geranyl diphosphate synthase in leaves of Pelargonium roseum, Phytochemistry (Oxf.) 30, 1757-1761.
    • (1991) Phytochemistry (Oxf.) , vol.30 , pp. 1757-1761
    • Suga, T.1    Endo, T.2
  • 47
    • 0028201454 scopus 로고
    • A human promyelocyte mRNA transiently induced by TPA is homologous to yeast IPP isomerase
    • Xuan, J. W., Kowalski, J., Chambers, A. F. & Denhardt, D. T. (1994) A human promyelocyte mRNA transiently induced by TPA is homologous to yeast IPP isomerase, Genomics 20, 129-131.
    • (1994) Genomics , vol.20 , pp. 129-131
    • Xuan, J.W.1    Kowalski, J.2    Chambers, A.F.3    Denhardt, D.T.4


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