메뉴 건너뛰기




Volumn 34, Issue C, 2000, Pages 191-247

Chapter Seven The biosynthesis, degradation, transport and possible function of cyanogenic glucosides

Author keywords

[No Author keywords available]

Indexed keywords


EID: 77957813628     PISSN: 00799920     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0079-9920(00)80008-8     Document Type: Chapter
Times cited : (42)

References (249)
  • 1
    • 0345522773 scopus 로고
    • Cyanogenic glucosides
    • Conn E.E. Cyanogenic glucosides. J. Agr. Food Chem. 7 (1969) 519-526
    • (1969) J. Agr. Food Chem. , vol.7 , pp. 519-526
    • Conn, E.E.1
  • 2
    • 0003109747 scopus 로고
    • Isolation and characterization of naturally occurring cyanogenic compounds
    • Seigler D.S. Isolation and characterization of naturally occurring cyanogenic compounds. Phytochemistry 14 (1975) 9-29
    • (1975) Phytochemistry , vol.14 , pp. 9-29
    • Seigler, D.S.1
  • 3
    • 0000248377 scopus 로고
    • Cyanogenic glucosides
    • Stumpf P.K., and Conn E.E. (Eds), Academic Press, New York
    • Conn E.E. Cyanogenic glucosides. In: Stumpf P.K., and Conn E.E. (Eds). Secondary Plant Products. The Biochemistry of Plants (1981), Academic Press, New York 479-500
    • (1981) Secondary Plant Products. The Biochemistry of Plants , pp. 479-500
    • Conn, E.E.1
  • 4
    • 0000026228 scopus 로고
    • Cyanogenesis in plants
    • Poulton J.E. Cyanogenesis in plants. Plant Physiol. 94 (1990) 401-405
    • (1990) Plant Physiol. , vol.94 , pp. 401-405
    • Poulton, J.E.1
  • 5
    • 0001324275 scopus 로고
    • Cyanogenic glucosides
    • Lea P.J. (Ed), Academic Press, New York
    • Møller B.L., and Poulton J. Cyanogenic glucosides. In: Lea P.J. (Ed). Methods of Plant Biochemistry Vol. 9 (1993), Academic Press, New York 183-207
    • (1993) Methods of Plant Biochemistry , vol.9 , pp. 183-207
    • Møller, B.L.1    Poulton, J.2
  • 6
    • 0000006728 scopus 로고    scopus 로고
    • Cyanogenic glucosides
    • Ikan R. (Ed), John Wiley and Sons, Toronto
    • Lechtenberg M., and Nahrstedt A. Cyanogenic glucosides. In: Ikan R. (Ed). Naturally Occurring Glycosides (1999), John Wiley and Sons, Toronto 147-191
    • (1999) Naturally Occurring Glycosides , pp. 147-191
    • Lechtenberg, M.1    Nahrstedt, A.2
  • 7
    • 0002970532 scopus 로고    scopus 로고
    • Biosynthesis of cyanogenic glucosides, cyanolipids, and related compunds
    • Plant Amino Acids. Singh B.K. (Ed)
    • Møller B.L., and Seigler D.S. Biosynthesis of cyanogenic glucosides, cyanolipids, and related compunds. In: Singh B.K. (Ed). Plant Amino Acids. Biochemistry and Biotechnology (1999) 563-609
    • (1999) Biochemistry and Biotechnology , pp. 563-609
    • Møller, B.L.1    Seigler, D.S.2
  • 8
    • 0009968269 scopus 로고
    • Characterisation of cyanogenic glycosides, cyanolipids, nitroglycosides, organic nitro compounds and nitrile glucosides from plants
    • Alkaloids and Sulphur Compounds. Waterman P.G., Dey P.M., and Harborne J.B. (Eds), Academic Press, New York
    • Seigler D.S., and Brinker A.M. Characterisation of cyanogenic glycosides, cyanolipids, nitroglycosides, organic nitro compounds and nitrile glucosides from plants. In: Waterman P.G., Dey P.M., and Harborne J.B. (Eds). Alkaloids and Sulphur Compounds. Meth. Plant Biochem. Volume 8 (1993), Academic Press, New York 51-131
    • (1993) Meth. Plant Biochem. , vol.8 , pp. 51-131
    • Seigler, D.S.1    Brinker, A.M.2
  • 9
    • 0008165851 scopus 로고
    • Novel b-cyanoglucosides in the epidermal tissue of barley and their possible role in the barley-powdery mildew interaction
    • Pourmohseni H., and Ibenthal W.D. Novel b-cyanoglucosides in the epidermal tissue of barley and their possible role in the barley-powdery mildew interaction. Angew. Bot. 65 (1991) 341-350
    • (1991) Angew. Bot. , vol.65 , pp. 341-350
    • Pourmohseni, H.1    Ibenthal, W.D.2
  • 11
    • 0000480371 scopus 로고
    • Subcellular localization of dhurrin β-glucosidase and hydroxynitrile lyase in the mesophyll cells of Sorghum leaf blades
    • Thayer S.S., and Conn E.E. Subcellular localization of dhurrin β-glucosidase and hydroxynitrile lyase in the mesophyll cells of Sorghum leaf blades. Plant Physiol. 67 (1981) 617-622
    • (1981) Plant Physiol. , vol.67 , pp. 617-622
    • Thayer, S.S.1    Conn, E.E.2
  • 12
    • 77957809797 scopus 로고
    • Subcellular localization of a UDP-glucose: aldehyde cyanohydrin β-glucosyl transferase in epidermal plastids of Sorghum leaf blades
    • Wurtele E.S., Thayer S.S., and Conn E.E. Subcellular localization of a UDP-glucose: aldehyde cyanohydrin β-glucosyl transferase in epidermal plastids of Sorghum leaf blades. Plant Physiol. 70 (1982) 1732-1737
    • (1982) Plant Physiol. , vol.70 , pp. 1732-1737
    • Wurtele, E.S.1    Thayer, S.S.2    Conn, E.E.3
  • 13
    • 0024259550 scopus 로고
    • Localization and catabolism of cyanogenic glucosides
    • Evered D., and Harnett S. (Eds), John Wiley & Sons, Chichester, UK
    • Poulton J.E. Localization and catabolism of cyanogenic glucosides. In: Evered D., and Harnett S. (Eds). Cyanide Compounds in Biology. Ciba Foundation Symposium 140 (1988), John Wiley & Sons, Chichester, UK 67-91
    • (1988) Cyanide Compounds in Biology. Ciba Foundation Symposium 140 , pp. 67-91
    • Poulton, J.E.1
  • 14
    • 0000392196 scopus 로고
    • In-situ localization of cyanogenic β-glucosidase (linamarase) gene expression in leaves of casava (Manihot esculenta Crantz) using non-isotopic riboprobes
    • Pancoro A., and Hughes M.A. In-situ localization of cyanogenic β-glucosidase (linamarase) gene expression in leaves of casava (Manihot esculenta Crantz) using non-isotopic riboprobes. Plant J. 2 (1992) 821-827
    • (1992) Plant J. , vol.2 , pp. 821-827
    • Pancoro, A.1    Hughes, M.A.2
  • 15
    • 0001059769 scopus 로고
    • Tissue and subcellular localization of enzymes catabolizing (R)-amygdalin in mature Prunus serotina seeds
    • Swain E., Li C.P., and Poulton J.E. Tissue and subcellular localization of enzymes catabolizing (R)-amygdalin in mature Prunus serotina seeds. Plant Physiol. 100 (1992) 291-300
    • (1992) Plant Physiol. , vol.100 , pp. 291-300
    • Swain, E.1    Li, C.P.2    Poulton, J.E.3
  • 16
    • 0028105773 scopus 로고
    • Utilization of amygdalin during seedling development of Prunus serotina
    • Swain E., and Poulton J.E. Utilization of amygdalin during seedling development of Prunus serotina. Plant Physiol. 106 (1994) 437-445
    • (1994) Plant Physiol. , vol.106 , pp. 437-445
    • Swain, E.1    Poulton, J.E.2
  • 17
    • 0001384282 scopus 로고
    • Distribution of cyanogenic potential in cassava germplasm
    • Bokanga M. Distribution of cyanogenic potential in cassava germplasm. Acta Hort. 375 (1994) 117-123
    • (1994) Acta Hort. , vol.375 , pp. 117-123
    • Bokanga, M.1
  • 19
    • 0025055402 scopus 로고
    • Konzo, an epidemic upper motor neuron disease studied in Tanzania
    • Howlett P., Brubaker G.R., Mlingi N., and Rosling H. Konzo, an epidemic upper motor neuron disease studied in Tanzania. Brain 113 (1990) 223-235
    • (1990) Brain , vol.113 , pp. 223-235
    • Howlett, P.1    Brubaker, G.R.2    Mlingi, N.3    Rosling, H.4
  • 20
    • 0026767790 scopus 로고
    • An outbreak of acute intoxications from consumption of insufficiently processed cassava in Tanzania
    • Mlingi N. An outbreak of acute intoxications from consumption of insufficiently processed cassava in Tanzania. Nutrition Res. 12 (1992) 677-687
    • (1992) Nutrition Res. , vol.12 , pp. 677-687
    • Mlingi, N.1
  • 21
    • 0001743005 scopus 로고
    • Measuring effects in humans of dietary cyanide exposure from cassava
    • Rosling H. Measuring effects in humans of dietary cyanide exposure from cassava. Acta Hort. 375 (1994) 271-283
    • (1994) Acta Hort. , vol.375 , pp. 271-283
    • Rosling, H.1
  • 22
    • 0024223050 scopus 로고
    • Cyanogenesis in animal-plant interactions
    • Cyanide Compounds in Biology. Evered D., and Harnett S. (Eds), John Wiley & Sons, Chichester, UK
    • Jones D.A. Cyanogenesis in animal-plant interactions. In: Evered D., and Harnett S. (Eds). Cyanide Compounds in Biology. Ciba Foundation Symposium 140 (1988), John Wiley & Sons, Chichester, UK 151-176
    • (1988) Ciba Foundation Symposium 140 , pp. 151-176
    • Jones, D.A.1
  • 23
    • 0000966890 scopus 로고
    • Mobilization and utilization of cyanogenic glucosides. The linustatin pathway
    • Selmar D., Lieberei R., and Biehl B. Mobilization and utilization of cyanogenic glucosides. The linustatin pathway. Plant Physiol. 86 (1988) 711-716
    • (1988) Plant Physiol. , vol.86 , pp. 711-716
    • Selmar, D.1    Lieberei, R.2    Biehl, B.3
  • 26
    • 0031985773 scopus 로고    scopus 로고
    • Why are so many food plants cyanogenic?
    • Jones D. Why are so many food plants cyanogenic?. Phytochemistry 47 (1998) 155-162
    • (1998) Phytochemistry , vol.47 , pp. 155-162
    • Jones, D.1
  • 27
    • 0027967537 scopus 로고
    • TYR , which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench
    • TYR , which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. Proc. Natl. Acad. Sci. USA 91 (1994) 9740-9744
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9740-9744
    • Sibbesen, O.1    Koch, B.2    Halkier, B.3    Møller, B.L.4
  • 28
    • 0029414488 scopus 로고
    • TYR , a multi-functional haem-thiolate N-hydroxylase involved in the biosynthesis of the cyanogenic glucoside dhurrin
    • TYR , a multi-functional haem-thiolate N-hydroxylase involved in the biosynthesis of the cyanogenic glucoside dhurrin. Drug Metab. Drug Interact. 12 (1995) 285-297
    • (1995) Drug Metab. Drug Interact. , vol.12 , pp. 285-297
    • Halkier, B.A.1    Sibbesen, O.2    Koch, B.3    Møller, B.L.4
  • 29
    • 0028834385 scopus 로고
    • The primary sequence of cytochrome P450tyr, the multifunctional N-hydroxylase catalyzing conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench
    • Koch B., Sibbesen O., Halkier B.A., Svendsen I., and Møller B.L. The primary sequence of cytochrome P450tyr, the multifunctional N-hydroxylase catalyzing conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. Arch. Biochem. Biophys. 323 (1995) 177-186
    • (1995) Arch. Biochem. Biophys. , vol.323 , pp. 177-186
    • Koch, B.1    Sibbesen, O.2    Halkier, B.A.3    Svendsen, I.4    Møller, B.L.5
  • 30
    • 0028985451 scopus 로고
    • TYR is a multifunctional heme-thiolate enzyme catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench
    • TYR is a multifunctional heme-thiolate enzyme catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. J. Biol. Chem. 270 (1995) 3506-3511
    • (1995) J. Biol. Chem. , vol.270 , pp. 3506-3511
    • Sibbesen, O.1    Koch, B.2    Halkier, B.A.3    Møller, B.L.4
  • 31
    • 0031397803 scopus 로고    scopus 로고
    • Isolation and reconstitution of cytochrome P450ox and in vitro reconstitution of the entire biosynthetic pathway of the cyanogenic glucoside dhurrin from sorghum
    • Kahn R., Bak S., Svendsen I., Halkier B.A., and Møller B.L. Isolation and reconstitution of cytochrome P450ox and in vitro reconstitution of the entire biosynthetic pathway of the cyanogenic glucoside dhurrin from sorghum. Plant Physiol. 115 (1997) 1661-1670
    • (1997) Plant Physiol. , vol.115 , pp. 1661-1670
    • Kahn, R.1    Bak, S.2    Svendsen, I.3    Halkier, B.A.4    Møller, B.L.5
  • 32
    • 0032005917 scopus 로고    scopus 로고
    • Cloning of three novel A-type cytochromes P450, CYP71E1, CYP98 and CYP99 from Sorghum bicolor (L.) Moench using a PCR approach and identification by expression in Escherichia coli of CYP71E1 as a multifunctional cytochrome P450 in the biosynthesis of the cyanogenic glucoside dhurrin
    • Bak S., Kahn R.A., Nielsen H.L., Møller B.L., and Halkier B.A. Cloning of three novel A-type cytochromes P450, CYP71E1, CYP98 and CYP99 from Sorghum bicolor (L.) Moench using a PCR approach and identification by expression in Escherichia coli of CYP71E1 as a multifunctional cytochrome P450 in the biosynthesis of the cyanogenic glucoside dhurrin. Plant Mol. Biol. 36 (1998) 393-405
    • (1998) Plant Mol. Biol. , vol.36 , pp. 393-405
    • Bak, S.1    Kahn, R.A.2    Nielsen, H.L.3    Møller, B.L.4    Halkier, B.A.5
  • 33
    • 77957790463 scopus 로고    scopus 로고
    • The UDP-glucose-p-hydroxymandelonitrile-O-glucosyltransferase that catalyzes the last step in synthesis of the cyanogenic glucoside dhurrin in Sorghum
    • In press
    • In press. Jones P.R., Møller B.L., and Høj P.B. The UDP-glucose-p-hydroxymandelonitrile-O-glucosyltransferase that catalyzes the last step in synthesis of the cyanogenic glucoside dhurrin in Sorghum. J. Biol. Chem. (2000)
    • (2000) J. Biol. Chem.
    • Jones, P.R.1    Møller, B.L.2    Høj, P.B.3
  • 34
    • 0001897157 scopus 로고
    • The molecular genetics of plant cyanogenic β-glucosidases
    • β-Glucosidases. Esen A. (Ed)
    • Hughes M.A. The molecular genetics of plant cyanogenic β-glucosidases. In: Esen A. (Ed). β-Glucosidases. ACS Symposium Series 533, Washington (1993) 153-169
    • (1993) ACS Symposium Series 533, Washington , pp. 153-169
    • Hughes, M.A.1
  • 35
    • 0029645413 scopus 로고
    • The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase
    • Barrett T., Suresh C.G., Tolley S.P., Dodson E.J., and Hughes M.A. The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase. Structure 3 (1995) 951-960
    • (1995) Structure , vol.3 , pp. 951-960
    • Barrett, T.1    Suresh, C.G.2    Tolley, S.P.3    Dodson, E.J.4    Hughes, M.A.5
  • 36
    • 0028247273 scopus 로고
    • Purification, characterization, and cloning of α-hydroxynitrile lyase from cassava (Manihot esculenta Crantz)
    • Hughes J., Dec. Carvalho F.J.P., and Hughes M.A. Purification, characterization, and cloning of α-hydroxynitrile lyase from cassava (Manihot esculenta Crantz). Arch. Biochem. Biophys. 311 (1994) 496-502
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 496-502
    • Hughes, J.1    Dec. Carvalho, F.J.P.2    Hughes, M.A.3
  • 37
    • 0029188401 scopus 로고
    • Purification and characterization of a novel (R)-mandelonitrile lyase from the fern Phlebodium aureum
    • Wajant H., Förster S., Selmar D., Effenberger F., and Pfizenmaier K. Purification and characterization of a novel (R)-mandelonitrile lyase from the fern Phlebodium aureum. Plant Physiol. 109 (1995) 1231-1238
    • (1995) Plant Physiol. , vol.109 , pp. 1231-1238
    • Wajant, H.1    Förster, S.2    Selmar, D.3    Effenberger, F.4    Pfizenmaier, K.5
  • 38
    • 0031397587 scopus 로고    scopus 로고
    • Sequencing, genomic organization, and preliminary promotor analysis of a black cherry (R)-(+)-mandelonitrile lyase gene
    • Hu Z., and Poulton J.E. Sequencing, genomic organization, and preliminary promotor analysis of a black cherry (R)-(+)-mandelonitrile lyase gene. Plant Physiol. 115 (1997) 1359-1369
    • (1997) Plant Physiol. , vol.115 , pp. 1359-1369
    • Hu, Z.1    Poulton, J.E.2
  • 39
    • 0031051520 scopus 로고    scopus 로고
    • Molecular cloning of acetone cyanhydrin lyase from flax (Linum usitatissimum. Definition of a novel class of hydroxynitrile lyases
    • Trummler K., and Wajant H. Molecular cloning of acetone cyanhydrin lyase from flax (Linum usitatissimum. Definition of a novel class of hydroxynitrile lyases. J. Biol. Chem. 272 (1997) 4770-4774
    • (1997) J. Biol. Chem. , vol.272 , pp. 4770-4774
    • Trummler, K.1    Wajant, H.2
  • 40
    • 0033117685 scopus 로고    scopus 로고
    • Molecular analysis of (R)-(+)-Mandelonitrile lyase microheterogeneity in black cherry
    • Hu Z., and Poulton J.E. Molecular analysis of (R)-(+)-Mandelonitrile lyase microheterogeneity in black cherry. Plant Physiol. 119 (1999) 1535-1546
    • (1999) Plant Physiol. , vol.119 , pp. 1535-1546
    • Hu, Z.1    Poulton, J.E.2
  • 41
    • 0001414090 scopus 로고
    • Studies on cyanogenic glycoside of sorghum vulgare
    • Akazawa T., Miljanich P., and Conn E.E. Studies on cyanogenic glycoside of sorghum vulgare. Plant Physiol. 35 (1960) 535-538
    • (1960) Plant Physiol. , vol.35 , pp. 535-538
    • Akazawa, T.1    Miljanich, P.2    Conn, E.E.3
  • 42
    • 0038142491 scopus 로고
    • Development of the potential for cyanogenesis in maturing black cherry (Prunus serotina Ehrh.) fruits
    • Swain E., Li C.P., and Poulton J.E. Development of the potential for cyanogenesis in maturing black cherry (Prunus serotina Ehrh.) fruits. Plant Physiol. 98 (1992) 1423-1428
    • (1992) Plant Physiol. , vol.98 , pp. 1423-1428
    • Swain, E.1    Li, C.P.2    Poulton, J.E.3
  • 43
    • 0033178673 scopus 로고    scopus 로고
    • Biosynthesis of cyanogenic glucosides in Triglochin maritima and the involvement of cytochrome P450 enzymes
    • Nielsen J.S., and Møller B.L. Biosynthesis of cyanogenic glucosides in Triglochin maritima and the involvement of cytochrome P450 enzymes. Arch. Biochem. Biophys. 368 (1999) 121-130
    • (1999) Arch. Biochem. Biophys. , vol.368 , pp. 121-130
    • Nielsen, J.S.1    Møller, B.L.2
  • 44
    • 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 8 (1996) 1821-1831
    • (1996) Plant Cell , vol.8 , pp. 1821-1831
    • Osbourn, A.E.1
  • 45
    • 0028906425 scopus 로고
    • The chemistry of defense: Theory and practice
    • Berenbaum M.R. The chemistry of defense: Theory and practice. Proc. Natl. Acad. Sci. USA 92 (1995) 2-8
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2-8
    • Berenbaum, M.R.1
  • 46
    • 0028095932 scopus 로고
    • Physiological roles for secondary metabolites in plants: Some progress, many outstanding problems
    • Rhodes M.J.C. Physiological roles for secondary metabolites in plants: Some progress, many outstanding problems. Plant Mol. Biol. 24 (1994) 1-20
    • (1994) Plant Mol. Biol. , vol.24 , pp. 1-20
    • Rhodes, M.J.C.1
  • 48
    • 0001733185 scopus 로고    scopus 로고
    • Plant cytochrome P450 monooxygenases
    • Schuler M.A. Plant cytochrome P450 monooxygenases. Crit. Rev. Plant Sci. 15 (1996) 235-284
    • (1996) Crit. Rev. Plant Sci. , vol.15 , pp. 235-284
    • Schuler, M.A.1
  • 49
    • 0025887421 scopus 로고
    • UDP-rhamnose: flavanone-7-O-glucoside-2″-O-rhamnosyltransferase. Purification and characterization of an enzyme catalyzing the production of bitter compounds in citrus
    • Bar-Peled M., Lewinsohn E., Fluhir R., and Gressel J. UDP-rhamnose: flavanone-7-O-glucoside-2″-O-rhamnosyltransferase. Purification and characterization of an enzyme catalyzing the production of bitter compounds in citrus. J. Biol. Chem. 266 (1991) 20953-20959
    • (1991) J. Biol. Chem. , vol.266 , pp. 20953-20959
    • Bar-Peled, M.1    Lewinsohn, E.2    Fluhir, R.3    Gressel, J.4
  • 50
    • 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
  • 51
    • 0000705071 scopus 로고
    • Efficient uptake of flavonoids into parsley (Petroselinum hortense) vacuoles requires acylated glycosides
    • Matern U., Reichenbach C., and Heller W. Efficient uptake of flavonoids into parsley (Petroselinum hortense) vacuoles requires acylated glycosides. Planta 167 (1986) 183-189
    • (1986) Planta , vol.167 , pp. 183-189
    • Matern, U.1    Reichenbach, C.2    Heller, W.3
  • 52
    • 0001723071 scopus 로고
    • Carrier-mediated uptake of 1-(malonylamino)-cyclopropane 1-carboxylic acid in vacuoles isolated from Catharanthus roseus cells
    • Bouzayen M., Latche A., Pech J.-C., and Marigo G. Carrier-mediated uptake of 1-(malonylamino)-cyclopropane 1-carboxylic acid in vacuoles isolated from Catharanthus roseus cells. Plant Physiol. 91 (1989) 1317-1322
    • (1989) Plant Physiol. , vol.91 , pp. 1317-1322
    • Bouzayen, M.1    Latche, A.2    Pech, J.-C.3    Marigo, G.4
  • 53
    • 0028129854 scopus 로고
    • A herbicide antidote (safener) induces the activity of both the herbicide tetoxifying enzyme and of a vacuolar transporter for the detoxified
    • Gaillard C., Dufaud A., Tommasini R., Kreuz K., Amrhein N., and Martinoia E. A herbicide antidote (safener) induces the activity of both the herbicide tetoxifying enzyme and of a vacuolar transporter for the detoxified. FEBS Lett. 352 (1994) 219-221
    • (1994) FEBS Lett. , vol.352 , pp. 219-221
    • Gaillard, C.1    Dufaud, A.2    Tommasini, R.3    Kreuz, K.4    Amrhein, N.5    Martinoia, E.6
  • 54
    • 0029909552 scopus 로고    scopus 로고
    • Different energization mechanisms drive the vacuolar uptake of a flavonoid glucoside and a herbicide glucoside
    • Klein M., Weissenböck G., Dufaud A., Gailliard C., Kreuz K., and Martinoia E. Different energization mechanisms drive the vacuolar uptake of a flavonoid glucoside and a herbicide glucoside. J. Biol. Chem. 271 (1996) 29666-29671
    • (1996) J. Biol. Chem. , vol.271 , pp. 29666-29671
    • Klein, M.1    Weissenböck, G.2    Dufaud, A.3    Gailliard, C.4    Kreuz, K.5    Martinoia, E.6
  • 55
    • 0029009655 scopus 로고
    • A glutathione S-transferase involved in vacuolar transfer encoded by the maize gene Bronze-2
    • Marrs K.A., Alfenito M.R., Lloyd A.M., and Walbat V. A glutathione S-transferase involved in vacuolar transfer encoded by the maize gene Bronze-2. Nature 375 (1995) 397-400
    • (1995) Nature , vol.375 , pp. 397-400
    • Marrs, K.A.1    Alfenito, M.R.2    Lloyd, A.M.3    Walbat, V.4
  • 56
    • 0031172678 scopus 로고    scopus 로고
    • Vacuolar uptake of the phytoalexin medicarpin by the glutathione conjugate pump
    • Li Z.-S., Alfenito M., Rea P.A., Walbot V., and Dixon R.A. Vacuolar uptake of the phytoalexin medicarpin by the glutathione conjugate pump. Phytochemistry 45 (1997) 689-693
    • (1997) Phytochemistry , vol.45 , pp. 689-693
    • Li, Z.-S.1    Alfenito, M.2    Rea, P.A.3    Walbot, V.4    Dixon, R.A.5
  • 57
    • 0028010294 scopus 로고
    • Herbicide safeners and glutathione metabolism
    • Farago S., Brunold C., and Kreuz K. Herbicide safeners and glutathione metabolism. Physiol. Plant. 91 (1994) 537-542
    • (1994) Physiol. Plant. , vol.91 , pp. 537-542
    • Farago, S.1    Brunold, C.2    Kreuz, K.3
  • 58
    • 0028020325 scopus 로고
    • Higher plant metabolism of xenobiotics: the "green liver" concept
    • Sandermann H. Higher plant metabolism of xenobiotics: the "green liver" concept. Pharmacogenetics 4 (1994) 225-241
    • (1994) Pharmacogenetics , vol.4 , pp. 225-241
    • Sandermann, H.1
  • 60
    • 0031127932 scopus 로고    scopus 로고
    • Detoxification of xenobiotics by plants: Chemical modification and vacuolar compartmentation
    • Coleman J.O.D., Blake-Kalff M.M.A., and Davies E.T.G. Detoxification of xenobiotics by plants: Chemical modification and vacuolar compartmentation. Trends Plant Sci. 2 (1997) 144-151
    • (1997) Trends Plant Sci. , vol.2 , pp. 144-151
    • Coleman, J.O.D.1    Blake-Kalff, M.M.A.2    Davies, E.T.G.3
  • 61
    • 0028019668 scopus 로고
    • Plant biochemistry of xenobiotics: Isolation and characterization of a soybean O-glucosyltransferase of DDT metabolism
    • Wetzel A., and Sandermann H. Plant biochemistry of xenobiotics: Isolation and characterization of a soybean O-glucosyltransferase of DDT metabolism. Arch. Biochem. Biophys. 314 (1994) 323-328
    • (1994) Arch. Biochem. Biophys. , vol.314 , pp. 323-328
    • Wetzel, A.1    Sandermann, H.2
  • 62
    • 0029110364 scopus 로고
    • Xenobiotic glucosyltransferase activity from suspension-cultured Glycine max cells
    • Gallandt E.R., and Balke N.E. Xenobiotic glucosyltransferase activity from suspension-cultured Glycine max cells. Pesticide Sci. 43 (1995) 31-40
    • (1995) Pesticide Sci. , vol.43 , pp. 31-40
    • Gallandt, E.R.1    Balke, N.E.2
  • 63
    • 0016260159 scopus 로고
    • The purification and properties of a uridine diphosphate glucose:aldehyde cyanohydrin β-glucosyltransferase from sorghum seedings
    • Reay P.F., and Conn E.E. The purification and properties of a uridine diphosphate glucose:aldehyde cyanohydrin β-glucosyltransferase from sorghum seedings. J. Biol. Chem. 249 (1974) 5826-5830
    • (1974) J. Biol. Chem. , vol.249 , pp. 5826-5830
    • Reay, P.F.1    Conn, E.E.2
  • 64
    • 0013615905 scopus 로고
    • Prunsin-6′-malonate, a cyanogenic glucoside from Merremia dissecta
    • Nahrstedt A., Skojottgaard Jensen P., and Wray V. Prunsin-6′-malonate, a cyanogenic glucoside from Merremia dissecta. Phytochemistry 28 (1989) 623-624
    • (1989) Phytochemistry , vol.28 , pp. 623-624
    • Nahrstedt, A.1    Skojottgaard Jensen, P.2    Wray, V.3
  • 65
    • 0005834127 scopus 로고
    • Developmental fate of the cyanogenic glucoside linamarin in Costa Rican wild lima bean seeds
    • Clegg D.O., Conn E.E., and Janzen D.H. Developmental fate of the cyanogenic glucoside linamarin in Costa Rican wild lima bean seeds. Nature 278 (1979) 343-344
    • (1979) Nature , vol.278 , pp. 343-344
    • Clegg, D.O.1    Conn, E.E.2    Janzen, D.H.3
  • 66
    • 0028253967 scopus 로고
    • Compartmentation of cyanogenic glucosides and their degrading enzymes
    • Gruhnert C., Biehl B., and Selmar D. Compartmentation of cyanogenic glucosides and their degrading enzymes. Planta 195 (1994) 36-42
    • (1994) Planta , vol.195 , pp. 36-42
    • Gruhnert, C.1    Biehl, B.2    Selmar, D.3
  • 67
    • 0022512771 scopus 로고
    • Clinical toxicology of cyanide
    • Hall A.H., and Rumack B.H. Clinical toxicology of cyanide. Ann. Emerg. Med. 15 (1986) 1067-1074
    • (1986) Ann. Emerg. Med. , vol.15 , pp. 1067-1074
    • Hall, A.H.1    Rumack, B.H.2
  • 68
    • 0000163181 scopus 로고
    • Cyanide as a metabolic inhibitor
    • Vennesland B., Conn E.E., Knowles C.J., Westley J., and Wissing F. (Eds), Academic Press, New York
    • Solomonson L.P. Cyanide as a metabolic inhibitor. In: Vennesland B., Conn E.E., Knowles C.J., Westley J., and Wissing F. (Eds). Cyanide in Biology (1981), Academic Press, New York 11-28
    • (1981) Cyanide in Biology , pp. 11-28
    • Solomonson, L.P.1
  • 69
    • 0014291604 scopus 로고
    • An ataxic neuropathy in Nigeria
    • Osuntukun B.O. An ataxic neuropathy in Nigeria. Brain 91 (1968) 215-245
    • (1968) Brain , vol.91 , pp. 215-245
    • Osuntukun, B.O.1
  • 70
    • 0026585473 scopus 로고
    • Cassava cyanogens and konzo, an upper motoneuron disease found in Africa
    • Tylleskär T., Banea M., Bikangi N., Cooke R., Poulter N.H., and Rosling H. Cassava cyanogens and konzo, an upper motoneuron disease found in Africa. Lancet 339 (1992) 208-211
    • (1992) Lancet , vol.339 , pp. 208-211
    • Tylleskär, T.1    Banea, M.2    Bikangi, N.3    Cooke, R.4    Poulter, N.H.5    Rosling, H.6
  • 72
    • 0019431358 scopus 로고
    • Amygdalin toxicity studies in rats predict cronic cyanide poisoning in humans
    • Netwon G.W., Schmidt E.S., Lewis J.P., Conn E.E., and Lawrence R. Amygdalin toxicity studies in rats predict cronic cyanide poisoning in humans. Western J. Med. 134 (1981) 97-103
    • (1981) Western J. Med. , vol.134 , pp. 97-103
    • Netwon, G.W.1    Schmidt, E.S.2    Lewis, J.P.3    Conn, E.E.4    Lawrence, R.5
  • 73
    • 0013045365 scopus 로고
    • Cyanogenesis in tropical feeds and foodstuffs
    • Vennesland B., Conn E.E., Knowles C.J., Westley J., and Wissing F. (Eds), Academic Press, New York
    • Nartey F. Cyanogenesis in tropical feeds and foodstuffs. In: Vennesland B., Conn E.E., Knowles C.J., Westley J., and Wissing F. (Eds). Cyanide in Biology (1981), Academic Press, New York 115-132
    • (1981) Cyanide in Biology , pp. 115-132
    • Nartey, F.1
  • 74
    • 84987291103 scopus 로고
    • Ethyl carbamate formation in graim based spirits. Part III. The primary source
    • Cook R., Mccaig N., McMillan J.M.b., and Lumsden W.B. Ethyl carbamate formation in graim based spirits. Part III. The primary source. J. Inst. Brew. 96 (1990) 233-244
    • (1990) J. Inst. Brew. , vol.96 , pp. 233-244
    • Cook, R.1    Mccaig, N.2    McMillan, J.M.b.3    Lumsden, W.B.4
  • 75
    • 0000588938 scopus 로고
    • Biological activity of dhurrin and other compounds from Johnson Grass (Sorghum halepense)
    • Nicollier G.F., Pope D.F., and Thompson A.C. Biological activity of dhurrin and other compounds from Johnson Grass (Sorghum halepense). J. Agr. Food Chem. 31 (1983) 744-748
    • (1983) J. Agr. Food Chem. , vol.31 , pp. 744-748
    • Nicollier, G.F.1    Pope, D.F.2    Thompson, A.C.3
  • 76
    • 0009830610 scopus 로고
    • Subcellular localization of the cyanogenic glucoside of sorghum by autoradiography
    • Saunders J.A., Conn E.E., Lin C.H., and Stocking R. Subcellular localization of the cyanogenic glucoside of sorghum by autoradiography. Plant Physiol. 59 (1977) 647-652
    • (1977) Plant Physiol. , vol.59 , pp. 647-652
    • Saunders, J.A.1    Conn, E.E.2    Lin, C.H.3    Stocking, R.4
  • 77
    • 0001213299 scopus 로고
    • Presence of the cyanogenic glucoside dhurrin in isolated vacuoles from sorghum
    • Saunders J.A., and Conn E.E. Presence of the cyanogenic glucoside dhurrin in isolated vacuoles from sorghum. Plant Physiol. 61 (1978) 154-157
    • (1978) Plant Physiol. , vol.61 , pp. 154-157
    • Saunders, J.A.1    Conn, E.E.2
  • 78
    • 0031046985 scopus 로고    scopus 로고
    • The effect of dietary plant glycosides on larval midgut β-glucosidases from Spodoptera frugiperda and Diatraea saccharalis
    • Ferreira C., Parra J.R.P., and Terra W.R. The effect of dietary plant glycosides on larval midgut β-glucosidases from Spodoptera frugiperda and Diatraea saccharalis. Insect Biochem. Mol. Biol. 27 (1997) 55-59
    • (1997) Insect Biochem. Mol. Biol. , vol.27 , pp. 55-59
    • Ferreira, C.1    Parra, J.R.P.2    Terra, W.R.3
  • 79
    • 84984117218 scopus 로고
    • Insect feeding on different sorghum cultivars in relation to cyanide and phenolic acid content
    • Woodhead S., Padgham D.E., and Bernays E.A. Insect feeding on different sorghum cultivars in relation to cyanide and phenolic acid content. Ann. Appl. Biol. 95 (1980) 151-157
    • (1980) Ann. Appl. Biol. , vol.95 , pp. 151-157
    • Woodhead, S.1    Padgham, D.E.2    Bernays, E.A.3
  • 80
    • 0002140025 scopus 로고
    • Cyanogenic compounds as protecting agents for organisms
    • Nahrstedt A. Cyanogenic compounds as protecting agents for organisms. Plant System. Evol. 150 (1985) 35-47
    • (1985) Plant System. Evol. , vol.150 , pp. 35-47
    • Nahrstedt, A.1
  • 81
    • 0000324991 scopus 로고
    • Cyanogenic glucosides as defense compounds. A review of the evidence
    • Hruska A.J. Cyanogenic glucosides as defense compounds. A review of the evidence. J. Chem. Ecol. 14 (1988) 2213-2217
    • (1988) J. Chem. Ecol. , vol.14 , pp. 2213-2217
    • Hruska, A.J.1
  • 82
    • 33846205807 scopus 로고
    • Presence of dhurrin in sorghum root tissue and the effect of pathogenesis on hydrogen cyanide potential
    • Starr J.L., Newton R.J., and Miller F.R. Presence of dhurrin in sorghum root tissue and the effect of pathogenesis on hydrogen cyanide potential. Crop Sci 24 (1984) 739-742
    • (1984) Crop Sci , vol.24 , pp. 739-742
    • Starr, J.L.1    Newton, R.J.2    Miller, F.R.3
  • 83
    • 0017648448 scopus 로고
    • Changes in release rates of cyanide in relation to palatability of Sorghum to insects
    • Woodhead S., and Bernays E. Changes in release rates of cyanide in relation to palatability of Sorghum to insects. Nature 270 (1977) 235-236
    • (1977) Nature , vol.270 , pp. 235-236
    • Woodhead, S.1    Bernays, E.2
  • 84
    • 0000323987 scopus 로고
    • The chemical basis of resistance of Sorghum bicolor to attack by Locusta migratoria
    • woodhead S., and Bernays E.A. The chemical basis of resistance of Sorghum bicolor to attack by Locusta migratoria. Ent. Exp. Appl. 24 (1978) 123-142
    • (1978) Ent. Exp. Appl. , vol.24 , pp. 123-142
    • woodhead, S.1    Bernays, E.A.2
  • 85
    • 0020870755 scopus 로고
    • Surface chemistry of Sorghum bicolor and its importance in feeding by Locusta migratoria
    • Woodhead S. Surface chemistry of Sorghum bicolor and its importance in feeding by Locusta migratoria. Physiol. Entomol. 8 (1983) 345-352
    • (1983) Physiol. Entomol. , vol.8 , pp. 345-352
    • Woodhead, S.1
  • 86
    • 0002114525 scopus 로고
    • p-Hydroxybenzaldehyde in the surface wax of sorghum: Its importance in seedling resistance to acridids
    • Woodhead S. p-Hydroxybenzaldehyde in the surface wax of sorghum: Its importance in seedling resistance to acridids. Ent. Exp. Appl. 31 (1982) 296-302
    • (1982) Ent. Exp. Appl. , vol.31 , pp. 296-302
    • Woodhead, S.1
  • 87
    • 0042504845 scopus 로고
    • Aphid feeding deterrents in sorghum. Bioassay, isolation and characterization
    • Dreyer D.L., Reese J.C., and Jones K.C. Aphid feeding deterrents in sorghum. Bioassay, isolation and characterization. J. Chem. Ecol. 7 (1981) 273-284
    • (1981) J. Chem. Ecol. , vol.7 , pp. 273-284
    • Dreyer, D.L.1    Reese, J.C.2    Jones, K.C.3
  • 88
    • 30444454767 scopus 로고
    • p-Hydroxybenzaldehyde as a major constituent of the epicuticular wax of seedling Sorghum bicolor
    • Woodhead S., Galeffi C., and Bettolo G.B.M. p-Hydroxybenzaldehyde as a major constituent of the epicuticular wax of seedling Sorghum bicolor. Phytochemistry 21 (1982) 455-456
    • (1982) Phytochemistry , vol.21 , pp. 455-456
    • Woodhead, S.1    Galeffi, C.2    Bettolo, G.B.M.3
  • 89
    • 0002812227 scopus 로고
    • Exogenous L-tyrosine metabolism and dhurrin turnover in sorghum seedlings
    • Bough W.A., and Gander J.E. Exogenous L-tyrosine metabolism and dhurrin turnover in sorghum seedlings. Phytochemistry 10 (1971) 67-77
    • (1971) Phytochemistry , vol.10 , pp. 67-77
    • Bough, W.A.1    Gander, J.E.2
  • 90
    • 0001205311 scopus 로고
    • Turnover of dhurrin in green sorghum seedlings
    • Adewusi S.R. Turnover of dhurrin in green sorghum seedlings. Plant Physiol. 94 (1990) 1219-1224
    • (1990) Plant Physiol. , vol.94 , pp. 1219-1224
    • Adewusi, S.R.1
  • 92
    • 0002545280 scopus 로고
    • a-Hydroxynitrile lyase in Hevea brasiliensis and its significance for rapid cyanogenesis
    • Selmar D., Lieberei R., Böhle B., and Conn E.E. a-Hydroxynitrile lyase in Hevea brasiliensis and its significance for rapid cyanogenesis. Physiol. Plant. 75 (1989) 97-101
    • (1989) Physiol. Plant. , vol.75 , pp. 97-101
    • Selmar, D.1    Lieberei, R.2    Böhle, B.3    Conn, E.E.4
  • 93
    • 0000713601 scopus 로고
    • Allelopathic potential of sorghum-sudangrass hybrid (SUDEX)
    • Weston L.A., Harmon R., and Mueller S. Allelopathic potential of sorghum-sudangrass hybrid (SUDEX). J. Chem. Ecol. 15 (1989) 1855-1865
    • (1989) J. Chem. Ecol. , vol.15 , pp. 1855-1865
    • Weston, L.A.1    Harmon, R.2    Mueller, S.3
  • 94
    • 0000617124 scopus 로고
    • Phytotoxicity of products from rhizospheres of a Sorghum-Sudangrass hybrid (Sorghum bicolor × Sorghum sudanese)
    • Forney D.R., and Foy C.L. Phytotoxicity of products from rhizospheres of a Sorghum-Sudangrass hybrid (Sorghum bicolor × Sorghum sudanese). Weed Sci. 33 (1985) 597-604
    • (1985) Weed Sci. , vol.33 , pp. 597-604
    • Forney, D.R.1    Foy, C.L.2
  • 95
    • 0009671536 scopus 로고
    • Acalyphin, a cyanogenic glucoside from Acalypha indica
    • Nahrstedt A., Kant J.D., and Wray V. Acalyphin, a cyanogenic glucoside from Acalypha indica. Phytochemistry 21 (1982) 101-105
    • (1982) Phytochemistry , vol.21 , pp. 101-105
    • Nahrstedt, A.1    Kant, J.D.2    Wray, V.3
  • 96
    • 0014291549 scopus 로고
    • Conversion of nitriles and α-hydroxynitriles to cyanogenic glucosides in flax seedlings and cherry laurel leaves
    • Hahlbrock K.H., Tapper B.A., Butler G.W., and Conn E.E. Conversion of nitriles and α-hydroxynitriles to cyanogenic glucosides in flax seedlings and cherry laurel leaves. Arch. Biochem. Biophys. 125 (1968) 1013-1016
    • (1968) Arch. Biochem. Biophys. , vol.125 , pp. 1013-1016
    • Hahlbrock, K.H.1    Tapper, B.A.2    Butler, G.W.3    Conn, E.E.4
  • 97
    • 0014939171 scopus 로고
    • The biosynthesis of cyanogenic glycosides in higher plants. Purification and properties of a uridine diphosphate-glucose-ketone cyanohydrin β-gluco-syltransferase from Linum usitatissium L
    • Hahlbrock K., and Conn E.E. The biosynthesis of cyanogenic glycosides in higher plants. Purification and properties of a uridine diphosphate-glucose-ketone cyanohydrin β-gluco-syltransferase from Linum usitatissium L. J. Biol. Chem. 245 (1970) 917-922
    • (1970) J. Biol. Chem. , vol.245 , pp. 917-922
    • Hahlbrock, K.1    Conn, E.E.2
  • 98
    • 0015132303 scopus 로고
    • Oximes, nitriles and 2-hydroxynitriles as precursors in the biosynthesis of cyanogenic glucosides
    • Tapper B.A., and Butler G.W. Oximes, nitriles and 2-hydroxynitriles as precursors in the biosynthesis of cyanogenic glucosides. Biochem. J. 124 (1971) 935-941
    • (1971) Biochem. J. , vol.124 , pp. 935-941
    • Tapper, B.A.1    Butler, G.W.2
  • 99
    • 49649138070 scopus 로고
    • Intermediates in the biosynthesis of linamarin
    • Tapper B.A., and Butler G.W. Intermediates in the biosynthesis of linamarin. Phytochemistry 11 (1972) 1041-1046
    • (1972) Phytochemistry , vol.11 , pp. 1041-1046
    • Tapper, B.A.1    Butler, G.W.2
  • 100
    • 49549164578 scopus 로고
    • Aldoximes and nitriles as intermediates in the biosynthesis of cyanogenic glucosides
    • Farnden K.J.G., Rosen M.A., and Liljegren D.R. Aldoximes and nitriles as intermediates in the biosynthesis of cyanogenic glucosides. Phytochemistry 12 (1973) 2673-2677
    • (1973) Phytochemistry , vol.12 , pp. 2673-2677
    • Farnden, K.J.G.1    Rosen, M.A.2    Liljegren, D.R.3
  • 101
    • 0016221504 scopus 로고
    • Stereochemical aspects of lotaustralin biosynthesis
    • Zilg H., and Conn E.E. Stereochemical aspects of lotaustralin biosynthesis. J. Biol. Chem. 249 (1974) 3112-3115
    • (1974) J. Biol. Chem. , vol.249 , pp. 3112-3115
    • Zilg, H.1    Conn, E.E.2
  • 102
    • 0016702052 scopus 로고
    • Stereochemical aspects of the biosynthesis of the epimeric cyanogenic glucosides dhurrin and taxiphyllin
    • Rosen M.A., Farnden K.J.F., and Conn E.E. Stereochemical aspects of the biosynthesis of the epimeric cyanogenic glucosides dhurrin and taxiphyllin. J. Biol. Chem. 250 (1975) 8302-8308
    • (1975) J. Biol. Chem. , vol.250 , pp. 8302-8308
    • Rosen, M.A.1    Farnden, K.J.F.2    Conn, E.E.3
  • 103
    • 0014010127 scopus 로고
    • The metabolism of aromatic compounds in higher plants. VII. The origin of the nitrile nitrogen atom of dhurrin (β-D0glucopyranosyloxy-L-p-hydroxymandelonitrile)
    • Uribe E.G., and Conn E.E. The metabolism of aromatic compounds in higher plants. VII. The origin of the nitrile nitrogen atom of dhurrin (β-D0glucopyranosyloxy-L-p-hydroxymandelonitrile). J. Biol. Chem. 241 (1966) 92-94
    • (1966) J. Biol. Chem. , vol.241 , pp. 92-94
    • Uribe, E.G.1    Conn, E.E.2
  • 104
    • 44949162266 scopus 로고
    • The metabolism of aromatic compounds in higher plants. VI: Studies on the biosynthesis of dhurrin, the cyanogenic glucoside of Sorghum vulgare
    • Koukol J., Miljanich P., and Conn E.E. The metabolism of aromatic compounds in higher plants. VI: Studies on the biosynthesis of dhurrin, the cyanogenic glucoside of Sorghum vulgare. J. Biol. Chem. 237 (1962) 3223-3228
    • (1962) J. Biol. Chem. , vol.237 , pp. 3223-3228
    • Koukol, J.1    Miljanich, P.2    Conn, E.E.3
  • 105
    • 0000571210 scopus 로고
    • Dhurrin synthesis in excised shoots and roots of sorghum seedlings
    • Reay P.F., and Conn E.E. Dhurrin synthesis in excised shoots and roots of sorghum seedlings. Phytochemistry 9 (1970) 1825-1827
    • (1970) Phytochemistry , vol.9 , pp. 1825-1827
    • Reay, P.F.1    Conn, E.E.2
  • 106
    • 0015750236 scopus 로고
    • Biosynthesis of cyanogenic glucosides
    • Conn E.E. Biosynthesis of cyanogenic glucosides. Biochem. Soc. Symp. 38 (1973) 277-302
    • (1973) Biochem. Soc. Symp. , vol.38 , pp. 277-302
    • Conn, E.E.1
  • 108
    • 0016833285 scopus 로고
    • The in vitro biosynthesis of dhurrin, the cyanogenic glucoside of Sorghum bicolor
    • McFarlane I.J., Lees E.M., and Conn E.E. The in vitro biosynthesis of dhurrin, the cyanogenic glucoside of Sorghum bicolor. J. Biol. Chem. 250 (1975) 4708-4713
    • (1975) J. Biol. Chem. , vol.250 , pp. 4708-4713
    • McFarlane, I.J.1    Lees, E.M.2    Conn, E.E.3
  • 109
    • 0002958809 scopus 로고
    • The biosynthesis of cyanogenic glucosides in higher plants. N-Hydroxytyrosine as an intermediate in the biosynthesis of dhurrin by Sorghum bicolor (Linn) Moench
    • Møller B.L., and Conn E.E. The biosynthesis of cyanogenic glucosides in higher plants. N-Hydroxytyrosine as an intermediate in the biosynthesis of dhurrin by Sorghum bicolor (Linn) Moench. J. Biol. Chem. 254 (1979) 8575-8583
    • (1979) J. Biol. Chem. , vol.254 , pp. 8575-8583
    • Møller, B.L.1    Conn, E.E.2
  • 110
    • 0003078891 scopus 로고
    • Biosynthesis of the cyanogenic glucoside dhurrin in seedlings of Sorghum bicolor (L.) Moench and partial purification of the enzyme system involved
    • Halkier B.A., and Møller B.L. Biosynthesis of the cyanogenic glucoside dhurrin in seedlings of Sorghum bicolor (L.) Moench and partial purification of the enzyme system involved. Plant Physiol. 90 (1989) 1552-1559
    • (1989) Plant Physiol. , vol.90 , pp. 1552-1559
    • Halkier, B.A.1    Møller, B.L.2
  • 111
    • 0040106748 scopus 로고
    • The biosynthesis of cyanogenic glucosides in higher plants. Channeling of intermediates in dhurrin biosynthesis by a microsomal systems from Sorghum bicolor (Linn) Moench
    • Møller B.L., and Conn E.E. The biosynthesis of cyanogenic glucosides in higher plants. Channeling of intermediates in dhurrin biosynthesis by a microsomal systems from Sorghum bicolor (Linn) Moench. J. Biol. Chem. 255 (1980) 3049-3056
    • (1980) J. Biol. Chem. , vol.255 , pp. 3049-3056
    • Møller, B.L.1    Conn, E.E.2
  • 112
    • 0025635902 scopus 로고
    • The biosynthesis of cyanogenic glucosides in higher plants. Identification of three hydroxylation steps in the biosynthesis of dhurrin in Sorghum bicolor (L.) Moench and the involvement of 1-aci-nitro-2-(p-hydroxyphenyl)ethane as an intermediate
    • Halkier B.A., and Møller B.L. The biosynthesis of cyanogenic glucosides in higher plants. Identification of three hydroxylation steps in the biosynthesis of dhurrin in Sorghum bicolor (L.) Moench and the involvement of 1-aci-nitro-2-(p-hydroxyphenyl)ethane as an intermediate. J. Biol. Chem. 265 (1990) 21114-21121
    • (1990) J. Biol. Chem. , vol.265 , pp. 21114-21121
    • Halkier, B.A.1    Møller, B.L.2
  • 113
    • 0022051560 scopus 로고
    • Properties of a microsomal enzyme system from Linum usitatissimum (linen flax) which oxidizes valine to acetone cyanohydrin and isoleucine to 2-methylbutanone cyanohydrin
    • Cutler A.J., Sternberg M., and Conn E.E. Properties of a microsomal enzyme system from Linum usitatissimum (linen flax) which oxidizes valine to acetone cyanohydrin and isoleucine to 2-methylbutanone cyanohydrin. Arch. Biochem. Biophys. 238 (1985) 272-279
    • (1985) Arch. Biochem. Biophys. , vol.238 , pp. 272-279
    • Cutler, A.J.1    Sternberg, M.2    Conn, E.E.3
  • 114
    • 0020198658 scopus 로고
    • In vitro characterization of the Ac locus in white clover (Trifoleum repens L.)
    • Collinge D.B., and Hughes M.A. In vitro characterization of the Ac locus in white clover (Trifoleum repens L.). Arch. Biochem. Biophys. 218 (1982) 38-45
    • (1982) Arch. Biochem. Biophys. , vol.218 , pp. 38-45
    • Collinge, D.B.1    Hughes, M.A.2
  • 115
    • 0019063918 scopus 로고
    • In vitro biosynthesis of the cyanogenic glucoside taxiphyllin in Triglochin maritima
    • Hösel W., and Nahrstedt A. In vitro biosynthesis of the cyanogenic glucoside taxiphyllin in Triglochin maritima. Arch. Biochem. Biophys. 203 (1980) 753-757
    • (1980) Arch. Biochem. Biophys. , vol.203 , pp. 753-757
    • Hösel, W.1    Nahrstedt, A.2
  • 116
    • 0019876872 scopus 로고
    • The in vitro biosynthesis of taxiphylin and the channeling of intermediates in Triglochin maritima
    • Cutler A.J., Hösel W., Sternberg M., and Conn E.E. The in vitro biosynthesis of taxiphylin and the channeling of intermediates in Triglochin maritima. J. Biol. Chem. 256 (1981) 4253-4258
    • (1981) J. Biol. Chem. , vol.256 , pp. 4253-4258
    • Cutler, A.J.1    Hösel, W.2    Sternberg, M.3    Conn, E.E.4
  • 117
    • 0342963733 scopus 로고
    • In-vitro biosynthesis of 1-(4′-hydroxyphenyl)-2-nitroethane and production of cyanogenic compounds in osmotically stressed cell suspension cultures of Eschscholtzia californica Cham
    • Hösel W., Berlin J., Hanzlik T.N., and Conn E.E. In-vitro biosynthesis of 1-(4′-hydroxyphenyl)-2-nitroethane and production of cyanogenic compounds in osmotically stressed cell suspension cultures of Eschscholtzia californica Cham. Plant 166 (1985) 176-181
    • (1985) Plant , vol.166 , pp. 176-181
    • Hösel, W.1    Berlin, J.2    Hanzlik, T.N.3    Conn, E.E.4
  • 118
    • 0026530834 scopus 로고
    • The biosynthesis of cyanogenic glucosides in seedlings of cassava (Manihot esculenta Crantz)
    • Koch B., Nielsen V.S., Halkier B.A., Olsen C.E., and Møller B.L. The biosynthesis of cyanogenic glucosides in seedlings of cassava (Manihot esculenta Crantz). Arch. Biochem. Biophys. 292 (1992) 141-150
    • (1992) Arch. Biochem. Biophys. , vol.292 , pp. 141-150
    • Koch, B.1    Nielsen, V.S.2    Halkier, B.A.3    Olsen, C.E.4    Møller, B.L.5
  • 119
    • 0017329528 scopus 로고
    • The enzymatic conversion of p-hydroxyphenylacetaldoxime to p-hydroxyphenylacetonitrile
    • Shimada M., and Conn E.E. The enzymatic conversion of p-hydroxyphenylacetaldoxime to p-hydroxyphenylacetonitrile. Arch. Biochem. Biophys. 180 (1977) 199-207
    • (1977) Arch. Biochem. Biophys. , vol.180 , pp. 199-207
    • Shimada, M.1    Conn, E.E.2
  • 120
    • 0024351594 scopus 로고
    • The biosynthesis of cyanogenic glucosides in higher plants. The (E)- and (Z)-isomers of p- hydroxyphenylacetaldehyde oxime as intermediates in the biosynthesis of dhurrin in Sorghum bicolor (L.) Moench
    • Halkier B.A., Olsen C.E., and Møller B.L. The biosynthesis of cyanogenic glucosides in higher plants. The (E)- and (Z)-isomers of p- hydroxyphenylacetaldehyde oxime as intermediates in the biosynthesis of dhurrin in Sorghum bicolor (L.) Moench. J. Biol. Chem. 264 (1989) 19487-19494
    • (1989) J. Biol. Chem. , vol.264 , pp. 19487-19494
    • Halkier, B.A.1    Olsen, C.E.2    Møller, B.L.3
  • 121
    • 0013594998 scopus 로고
    • Chemical synthesis and disproportionation of N-hydroxytyrosine
    • Møller B.L., Mcfarlane I.J., and Conn E.E. Chemical synthesis and disproportionation of N-hydroxytyrosine. Acta Chem. Scand. B31 (1977) 343-344
    • (1977) Acta Chem. Scand. , vol.B31 , pp. 343-344
    • Møller, B.L.1    Mcfarlane, I.J.2    Conn, E.E.3
  • 122
    • 0017392161 scopus 로고
    • Intermediates in the biosynthesis of cyanogenic glucosides determined by use of a gas chromatograph coupled with a gas proportional counter
    • Møller B.L. Intermediates in the biosynthesis of cyanogenic glucosides determined by use of a gas chromatograph coupled with a gas proportional counter. Anal. Biochem. 81 (1978) 292-304
    • (1978) Anal. Biochem. , vol.81 , pp. 292-304
    • Møller, B.L.1
  • 123
    • 51849177764 scopus 로고
    • Mass spectrometric identification of intermediates in the biosynthesis of cyanogenic glucosides
    • Møller B.L., Conn E.E., and Sweeley C.C. Mass spectrometric identification of intermediates in the biosynthesis of cyanogenic glucosides. Carlsberg Res. Commun. 44 (1979) 367-379
    • (1979) Carlsberg Res. Commun. , vol.44 , pp. 367-379
    • Møller, B.L.1    Conn, E.E.2    Sweeley, C.C.3
  • 124
    • 0004254526 scopus 로고
    • The involvement of N-hydroxyamino acids as intermediates in metabolic transformations
    • Vennesland B., Conn E.E., Knowles C.J., Westley J., and Wissing F. (Eds), Academic Press, London
    • Møller B.L. The involvement of N-hydroxyamino acids as intermediates in metabolic transformations. In: Vennesland B., Conn E.E., Knowles C.J., Westley J., and Wissing F. (Eds). Cyanide in Biology (1981), Academic Press, London 197-215
    • (1981) Cyanide in Biology , pp. 197-215
    • Møller, B.L.1
  • 125
    • 0025965049 scopus 로고
    • 2-Nitro-3-(p-hydroxy-phenyl)propionate and aci-1-nitro-2-(p-hydroxyphenyl)ethane, two intermediates in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench
    • Halkier B.A., Lykkesfeldt J., and Møller B.L. 2-Nitro-3-(p-hydroxy-phenyl)propionate and aci-1-nitro-2-(p-hydroxyphenyl)ethane, two intermediates in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. Proc. Natl. Acad. Sci. USA 88 (1991) 487-491
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 487-491
    • Halkier, B.A.1    Lykkesfeldt, J.2    Møller, B.L.3
  • 126
    • 12044256272 scopus 로고
    • Involvement of cytochrome P-450 in the biosynthesis of dhurrin in Sorghum bicolor (L.) Moench
    • Halkier B.A., and Møller B.L. Involvement of cytochrome P-450 in the biosynthesis of dhurrin in Sorghum bicolor (L.) Moench. Plant Physiol. 96 (1990) 10-17
    • (1990) Plant Physiol. , vol.96 , pp. 10-17
    • Halkier, B.A.1    Møller, B.L.2
  • 127
    • 0000415929 scopus 로고
    • The reaction of pyridine nucleotide with cyanide and its analytical use
    • Colowick S.P., Kaplan N.O., and Ciotti M. The reaction of pyridine nucleotide with cyanide and its analytical use. J. Biol. Chem. 191 (1951) 447-459
    • (1951) J. Biol. Chem. , vol.191 , pp. 447-459
    • Colowick, S.P.1    Kaplan, N.O.2    Ciotti, M.3
  • 128
    • 0024222871 scopus 로고
    • Cyanogenic glucosides: the biosynthetic pathway and the enzyme system involved
    • Cyanide Compounds in Biology. Evered D., and Harnet S. (Eds), J. Wiley, Chichester
    • Halkier B.A., Scheller H.V., and Møller B.L. Cyanogenic glucosides: the biosynthetic pathway and the enzyme system involved. In: Evered D., and Harnet S. (Eds). Cyanide Compounds in Biology. Ciba Found. Symp. 140 (1988), J. Wiley, Chichester 49-66
    • (1988) Ciba Found. Symp. , vol.140 , pp. 49-66
    • Halkier, B.A.1    Scheller, H.V.2    Møller, B.L.3
  • 129
    • 0000737257 scopus 로고
    • Multiple forms of plant cytochromes P-450
    • Donaldson R.P., and Luster D.G. Multiple forms of plant cytochromes P-450. Plant Physiol. 96 (1991) 669-674
    • (1991) Plant Physiol. , vol.96 , pp. 669-674
    • Donaldson, R.P.1    Luster, D.G.2
  • 130
    • 0030239348 scopus 로고    scopus 로고
    • Catalytic reactivities and structure/function relationships of cytochrome P450 enzymes
    • Halkier B.A. Catalytic reactivities and structure/function relationships of cytochrome P450 enzymes. Phytochemistry 43 (1996) 1-21
    • (1996) Phytochemistry , vol.43 , pp. 1-21
    • Halkier, B.A.1
  • 131
    • 0023918714 scopus 로고
    • On the membrane topology of vertebrate cytochrome P-450 proteins
    • Nelson D.R., and Strobel H.W. On the membrane topology of vertebrate cytochrome P-450 proteins. J. Biol. Chem. 263 (1988) 6038-6050
    • (1988) J. Biol. Chem. , vol.263 , pp. 6038-6050
    • Nelson, D.R.1    Strobel, H.W.2
  • 133
    • 0029586190 scopus 로고
    • Cytochromes P450 in the phenylpropanoid metabolism
    • Werck-Reichart D. Cytochromes P450 in the phenylpropanoid metabolism. Drug Metab. Drug Interact. 12 (1995) 221-243
    • (1995) Drug Metab. Drug Interact. , vol.12 , pp. 221-243
    • Werck-Reichart, D.1
  • 134
    • 0030111330 scopus 로고    scopus 로고
    • Cloning of wound induced cytochrome P450 monooxygenases expressed in pea
    • Frank M.R., Deyneka J.M., and Schuler M.A. Cloning of wound induced cytochrome P450 monooxygenases expressed in pea. Plant Physiol. 110 (1996) 1035-1046
    • (1996) Plant Physiol. , vol.110 , pp. 1035-1046
    • Frank, M.R.1    Deyneka, J.M.2    Schuler, M.A.3
  • 135
    • 0030975251 scopus 로고    scopus 로고
    • Regulation of the cinnamate 4-hydroxylase (CYP73A1) in Jerusalem artichoke, tubers in response to wounding and chemical treatments
    • Batard Y., Schalk M., Pierrel M.A., Zimmerlin A., Durst F., and Werck-Reichart D. Regulation of the cinnamate 4-hydroxylase (CYP73A1) in Jerusalem artichoke, tubers in response to wounding and chemical treatments. Plant Physiol. 113 (1997) 931-959
    • (1997) Plant Physiol. , vol.113 , pp. 931-959
    • Batard, Y.1    Schalk, M.2    Pierrel, M.A.3    Zimmerlin, A.4    Durst, F.5    Werck-Reichart, D.6
  • 138
    • 0032146134 scopus 로고    scopus 로고
    • Double Triton X-114 phase partitioning for the purification of plant cytochromes P450 and removal of green pigments
    • Andersen M.D., and Møller B.L. Double Triton X-114 phase partitioning for the purification of plant cytochromes P450 and removal of green pigments. Prot. Express. Purific. 13 (1998) 366-372
    • (1998) Prot. Express. Purific. , vol.13 , pp. 366-372
    • Andersen, M.D.1    Møller, B.L.2
  • 139
    • 0017794351 scopus 로고
    • Measurement of substrate and inhibitor binding to microsomal cytochrome P-450 by optical difference spectroscopy
    • Jefcote C.R. Measurement of substrate and inhibitor binding to microsomal cytochrome P-450 by optical difference spectroscopy. Methods Enzymol. 27 (1978) 258-279
    • (1978) Methods Enzymol. , vol.27 , pp. 258-279
    • Jefcote, C.R.1
  • 141
    • 0031079568 scopus 로고    scopus 로고
    • Cloning and expression in Escherichia coli of the obtusifoliol 14α-demethylase of Sorghum bicolor (L.) Moench, a cytochrome P450 orthologous of the lanosterol 14α-demethylases (CYP51) from fungi and mammals
    • Bak S., Kahn R.A., Olsen C.E., and Halkier B.A. Cloning and expression in Escherichia coli of the obtusifoliol 14α-demethylase of Sorghum bicolor (L.) Moench, a cytochrome P450 orthologous of the lanosterol 14α-demethylases (CYP51) from fungi and mammals. Plant J. 11 (1997) 191-201
    • (1997) Plant J. , vol.11 , pp. 191-201
    • Bak, S.1    Kahn, R.A.2    Olsen, C.E.3    Halkier, B.A.4
  • 142
    • 12644251864 scopus 로고    scopus 로고
    • Isolation and reconstitution of the heme-thiolate protein obtusifoliol 14α-demethylase from Sorghum bicolor (L.) Moench
    • Kahn R.A., Bak S., Olsen C.E., Svendsen I., and Møller B.L. Isolation and reconstitution of the heme-thiolate protein obtusifoliol 14α-demethylase from Sorghum bicolor (L.) Moench. J. Biol. Chem. 271 (1996) 32944-32950
    • (1996) J. Biol. Chem. , vol.271 , pp. 32944-32950
    • Kahn, R.A.1    Bak, S.2    Olsen, C.E.3    Svendsen, I.4    Møller, B.L.5
  • 143
    • 0033102583 scopus 로고    scopus 로고
    • Substrate specificity of the cytochrome P450 enzymes CYP79A1 and CYP71E1 involved in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench
    • Kahn R.A., and Møller B.L. Substrate specificity of the cytochrome P450 enzymes CYP79A1 and CYP71E1 involved in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. Arch. Biochem. Biophys. 363 (1999) 9-18
    • (1999) Arch. Biochem. Biophys. , vol.363 , pp. 9-18
    • Kahn, R.A.1    Møller, B.L.2
  • 145
    • 0029589359 scopus 로고
    • Functional and DNA sequence divergence of the CYP71 gene family in higher plants
    • Christofferson R.E., Percival F.W., and Bozak K. Functional and DNA sequence divergence of the CYP71 gene family in higher plants. Drug. Metab. Drug Interact. 12 (1995) 207-221
    • (1995) Drug. Metab. Drug Interact. , vol.12 , pp. 207-221
    • Christofferson, R.E.1    Percival, F.W.2    Bozak, K.3
  • 147
    • 0033199227 scopus 로고    scopus 로고
    • Cytochrome P450 and the individuality of species
    • Nelson D.R. Cytochrome P450 and the individuality of species. Arch. Biochem. Biophys. 369 (1999) 1-10
    • (1999) Arch. Biochem. Biophys. , vol.369 , pp. 1-10
    • Nelson, D.R.1
  • 148
    • 0025114542 scopus 로고
    • Isolation of two developmentally regulated genes involved in spore wall maturation in Saccharomyces cerevisiae
    • Briza P., Breitenbach M., Ellinger A., and Segall J. Isolation of two developmentally regulated genes involved in spore wall maturation in Saccharomyces cerevisiae. Gen. Dev. 4 (1990) 1775-1789
    • (1990) Gen. Dev. , vol.4 , pp. 1775-1789
    • Briza, P.1    Breitenbach, M.2    Ellinger, A.3    Segall, J.4
  • 149
    • 0034695491 scopus 로고    scopus 로고
    • Cytochromes P450 from cassava (Manihot esculenta Crantz) catalyzing the first steps in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin. Cloning, functional expression in Pichia pastoris and substrate specificity of the isolated recombinant enzymes
    • In press
    • In press. Andersen M.D., Busk P.K., Svendsen I., and Møller B.L. Cytochromes P450 from cassava (Manihot esculenta Crantz) catalyzing the first steps in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin. Cloning, functional expression in Pichia pastoris and substrate specificity of the isolated recombinant enzymes. J. Biol. Chem. (2000)
    • (2000) J. Biol. Chem.
    • Andersen, M.D.1    Busk, P.K.2    Svendsen, I.3    Møller, B.L.4
  • 150
    • 0025994649 scopus 로고
    • Expression and enzymatic activity of recombinant cytochrome P450 17α-hydroxylase in Escherichia coli
    • Barnes H.J., Arlotto M.P., and Waterman M.R. Expression and enzymatic activity of recombinant cytochrome P450 17α-hydroxylase in Escherichia coli. Proc. Natl. Acad. Sci. USA 88 (1991) 5597-5601
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5597-5601
    • Barnes, H.J.1    Arlotto, M.P.2    Waterman, M.R.3
  • 151
    • 0029757088 scopus 로고    scopus 로고
    • Maximizing expression of eucaryotic cytochrome P450s in Escherichia coli
    • Barnes H.J. Maximizing expression of eucaryotic cytochrome P450s in Escherichia coli. Methods Enzymol. 272 (1996) 3-14
    • (1996) Methods Enzymol. , vol.272 , pp. 3-14
    • Barnes, H.J.1
  • 153
    • 0029621245 scopus 로고
    • Diversity and evolution of plant P450 and P450-reductases
    • Durst F., and Nelson D.R. Diversity and evolution of plant P450 and P450-reductases. Drug Metab. Drug Interact. 12 (1995) 198-206
    • (1995) Drug Metab. Drug Interact. , vol.12 , pp. 198-206
    • Durst, F.1    Nelson, D.R.2
  • 155
    • 0028848836 scopus 로고
    • Expression of a cytochrome P450 gene family in maize
    • Frey M., Kliem R., Saedler H., and Gierl A. Expression of a cytochrome P450 gene family in maize. Mol. Gen. Genet. 246 (1995) 100-109
    • (1995) Mol. Gen. Genet. , vol.246 , pp. 100-109
    • Frey, M.1    Kliem, R.2    Saedler, H.3    Gierl, A.4
  • 156
    • 0001734363 scopus 로고
    • A Beckmann-type dehydration of n-butyraldoxime catalyzed by cytochrome P450
    • Demaster E.G., Shirota F.N., and Nagasawa H.T. A Beckmann-type dehydration of n-butyraldoxime catalyzed by cytochrome P450. J. Org. Chem. 57 (1992) 5074-5075
    • (1992) J. Org. Chem. , vol.57 , pp. 5074-5075
    • Demaster, E.G.1    Shirota, F.N.2    Nagasawa, H.T.3
  • 157
    • 0028240839 scopus 로고
    • Dehydration of alkyl- and arylaldoximes as a new cytochrome P450-catalyzed reaction: Mechanism and stereochemical characteristics
    • Boucher J.L., Delaforge M., and Mansuy D. Dehydration of alkyl- and arylaldoximes as a new cytochrome P450-catalyzed reaction: Mechanism and stereochemical characteristics. Biochemistry 33 (1994) 7811-7818
    • (1994) Biochemistry , vol.33 , pp. 7811-7818
    • Boucher, J.L.1    Delaforge, M.2    Mansuy, D.3
  • 158
    • 84961488509 scopus 로고
    • Cytochromes P450 and model systems: Great diversity of catalyzed reactions
    • Mansuy D. Cytochromes P450 and model systems: Great diversity of catalyzed reactions. Pure Appl. Chem. 66 (1994) 737-744
    • (1994) Pure Appl. Chem. , vol.66 , pp. 737-744
    • Mansuy, D.1
  • 160
    • 0023056493 scopus 로고
    • scc -substrate interactions. Role of the 3β- and side chain hydroxyls in binding to oxidized and reduced forms of the enzyme
    • scc -substrate interactions. Role of the 3β- and side chain hydroxyls in binding to oxidized and reduced forms of the enzyme. J. Biol. Chem. 261 (1986) 2743-2749
    • (1986) J. Biol. Chem. , vol.261 , pp. 2743-2749
    • Heyl, B.L.1    Tyrrell, D.J.2    Lambeth, J.D.3
  • 161
    • 2142645726 scopus 로고
    • On the absence of 2-(2′-cyclopentenyl)glycine-derived cyanogenic glucosides in cassava, Manihot esculenta Crantz
    • Lykkesfeldt J., and Møller B.L. On the absence of 2-(2′-cyclopentenyl)glycine-derived cyanogenic glucosides in cassava, Manihot esculenta Crantz. Acta Chem. Scand. 49 (1995) 540-542
    • (1995) Acta Chem. Scand. , vol.49 , pp. 540-542
    • Lykkesfeldt, J.1    Møller, B.L.2
  • 162
    • 0142102003 scopus 로고
    • Changes in cyanogenic glucoside content in seeds and seedlings of Hevea, species
    • Selmar D., Lieberei R., Junqueira N., and Biehl B. Changes in cyanogenic glucoside content in seeds and seedlings of Hevea, species. Phytochemistry 30 (1991) 2135-2140
    • (1991) Phytochemistry , vol.30 , pp. 2135-2140
    • Selmar, D.1    Lieberei, R.2    Junqueira, N.3    Biehl, B.4
  • 163
    • 0011315766 scopus 로고
    • Translocation of cyanogenic glucosides in cassava
    • Selmar D. Translocation of cyanogenic glucosides in cassava. Acta. Hort. 375 (1994) 61-67
    • (1994) Acta. Hort. , vol.375 , pp. 61-67
    • Selmar, D.1
  • 164
    • 0011216893 scopus 로고
    • Cyanogenic glucosides in cassava, Manihot esculenta Crantz
    • Lykkesfeldt J., and Møller B.L. Cyanogenic glucosides in cassava, Manihot esculenta Crantz. Acta Chem. Scand. 48 (1994) 178-180
    • (1994) Acta Chem. Scand. , vol.48 , pp. 178-180
    • Lykkesfeldt, J.1    Møller, B.L.2
  • 165
  • 166
    • 0029170839 scopus 로고
    • The biosynthesis of cyanogenic glucosides in roots of cassava
    • Du L., Bokanga M., Møller B.L., and Halkier B.A. The biosynthesis of cyanogenic glucosides in roots of cassava. Phytochemistry 39 (1995) 323-326
    • (1995) Phytochemistry , vol.39 , pp. 323-326
    • Du, L.1    Bokanga, M.2    Møller, B.L.3    Halkier, B.A.4
  • 167
    • 0008489294 scopus 로고
    • Possible use of a biotechnological approach to optimize and regulate the content and distribution of cyanogenic glucosides in cassava to increase food safety
    • Koch B.M., Sibbesen O., Swain E., Kahn R.A., Du L., Bak S., Halkier B.A., and Møller B.L. Possible use of a biotechnological approach to optimize and regulate the content and distribution of cyanogenic glucosides in cassava to increase food safety. Acta Hort 375 (1994) 45-60
    • (1994) Acta Hort , vol.375 , pp. 45-60
    • Koch, B.M.1    Sibbesen, O.2    Swain, E.3    Kahn, R.A.4    Du, L.5    Bak, S.6    Halkier, B.A.7    Møller, B.L.8
  • 168
    • 0033998717 scopus 로고    scopus 로고
    • Cloning and expression of cytochrome P450 catalyzing the conversion of tyrosine to p-hydroxyphenylacetaldoxime in the biosynthesis of cyanogenic glucosides in Triglochin maritima
    • in press
    • in press. Nielsen J.S., and Møller B.L. Cloning and expression of cytochrome P450 catalyzing the conversion of tyrosine to p-hydroxyphenylacetaldoxime in the biosynthesis of cyanogenic glucosides in Triglochin maritima. Plant Physiol. (2000)
    • (2000) Plant Physiol.
    • Nielsen, J.S.1    Møller, B.L.2
  • 169
    • 0029556989 scopus 로고
    • Involvement of a cytochrome P450 in glucosinolate biosynthesis as demonstrated by an in vitro microsomal enzyme system isolated from jasmonic acid-induced seedlings of Sinapis alba L
    • Du L., Lykkesfeldt J., Olsen C.E., and Halkier B.A. Involvement of a cytochrome P450 in glucosinolate biosynthesis as demonstrated by an in vitro microsomal enzyme system isolated from jasmonic acid-induced seedlings of Sinapis alba L. Proc. Natl. Acad. Sci. USA 92 (1995) 12505-12509
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12505-12509
    • Du, L.1    Lykkesfeldt, J.2    Olsen, C.E.3    Halkier, B.A.4
  • 170
    • 0032215492 scopus 로고    scopus 로고
    • The presence of CYP79 homologous in glucosinolate-producing plants shows evolutionary conservation of the enzymes in the conversion of amino acid to aldoxime in the biosynthesis of cyanogenc glucosides and glucosinolates
    • Bak S., Nielsen H.L., and Halkier B.A. The presence of CYP79 homologous in glucosinolate-producing plants shows evolutionary conservation of the enzymes in the conversion of amino acid to aldoxime in the biosynthesis of cyanogenc glucosides and glucosinolates. Plant Mol. Biol. 38 (1998) 724-734
    • (1998) Plant Mol. Biol. , vol.38 , pp. 724-734
    • Bak, S.1    Nielsen, H.L.2    Halkier, B.A.3
  • 171
    • 0023743926 scopus 로고
    • HPLC separation of glucosinolates from seeds and leaves of Arabidopsis thaliana and their identification using thermospray liquid chromatography-mass spectrometry
    • Hogge R.L., Reed D.W., and Underhill E.W. HPLC separation of glucosinolates from seeds and leaves of Arabidopsis thaliana and their identification using thermospray liquid chromatography-mass spectrometry. J. Chromatogr. Sci. 26 (1988) 551-560
    • (1988) J. Chromatogr. Sci. , vol.26 , pp. 551-560
    • Hogge, R.L.1    Reed, D.W.2    Underhill, E.W.3
  • 172
    • 0029643786 scopus 로고
    • Structure and function of cytochromes P450: A comparative analysis of three crystal structures
    • Hasemann C.A., Kurumbail R.G., Boddupalli S.S., Peterson J.A., and Deisenhofer J. Structure and function of cytochromes P450: A comparative analysis of three crystal structures. Structure 3 (1995) 41-62
    • (1995) Structure , vol.3 , pp. 41-62
    • Hasemann, C.A.1    Kurumbail, R.G.2    Boddupalli, S.S.3    Peterson, J.A.4    Deisenhofer, J.5
  • 173
    • 0026542989 scopus 로고
    • Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences
    • Gotoh O. Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences. J. Biol. Chem. 267 (1992) 83-90
    • (1992) J. Biol. Chem. , vol.267 , pp. 83-90
    • Gotoh, O.1
  • 174
    • 0027603825 scopus 로고
    • Isolation of cytochrome P-450 cDNA clones from the higher plant Catharanthus roseus by a PCR strategy
    • Meijer A.H., Souer E., Verpoorte R., and Hoge J.H.C. Isolation of cytochrome P-450 cDNA clones from the higher plant Catharanthus roseus by a PCR strategy. Plant Mol. Biol. 22 (1993) 379-383
    • (1993) Plant Mol. Biol. , vol.22 , pp. 379-383
    • Meijer, A.H.1    Souer, E.2    Verpoorte, R.3    Hoge, J.H.C.4
  • 176
    • 0023390030 scopus 로고
    • A short amino-terminal segment of microsomal cytochrome P-450 functions as an insertion signal and as a stop-transfer sequence
    • Sakaguchi M., Mihara K., and Sato R. A short amino-terminal segment of microsomal cytochrome P-450 functions as an insertion signal and as a stop-transfer sequence. EMBO J. 6 (1987) 2425-2431
    • (1987) EMBO J. , vol.6 , pp. 2425-2431
    • Sakaguchi, M.1    Mihara, K.2    Sato, R.3
  • 177
    • 0021762829 scopus 로고
    • Biosynthesis of cyanogenic glucosides: in vitro analysis of the glucosylation step
    • Hösel W., and Schiel O. Biosynthesis of cyanogenic glucosides: in vitro analysis of the glucosylation step. Arch. Biochem. Biophys. 229 (1984) 177-186
    • (1984) Arch. Biochem. Biophys. , vol.229 , pp. 177-186
    • Hösel, W.1    Schiel, O.2
  • 178
    • 0012752736 scopus 로고
    • Glucosyltransferases of the cyanogenic plant cassava (Manihot esculenta, Crantz)
    • Mederacke H., Selmar D., and Biehl B. Glucosyltransferases of the
    • (1995) Angew. Bot. , vol.69 , pp. 119-124
    • Mederacke, H.1    Selmar, D.2    Biehl, B.3
  • 179
    • 0030207724 scopus 로고    scopus 로고
    • Characterization of two cyano glucosyltransferases from cassava leaves
    • Mederacke H., Biehl B., and Selmar D. Characterization of two cyano glucosyltransferases from cassava leaves. Phytochemistry 42 (1996) 1517-1522
    • (1996) Phytochemistry , vol.42 , pp. 1517-1522
    • Mederacke, H.1    Biehl, B.2    Selmar, D.3
  • 180
    • 0000908396 scopus 로고
    • Glycosylation and glycosidases
    • Stumpf P.K., and Conn E.E. (Eds), Academic Press, New York
    • Hösel W. Glycosylation and glycosidases. In: Stumpf P.K., and Conn E.E. (Eds). The Biochemistry of Plants Vol. 7 (1981), Academic Press, New York 725-753
    • (1981) The Biochemistry of Plants , vol.7 , pp. 725-753
    • Hösel, W.1
  • 181
    • 0001784964 scopus 로고    scopus 로고
    • The analysis of flavouring compounds in grapes
    • Linskens H.F., and Jackson J.F. (Eds), Springer-Verlag, Berlin & Heidelberg
    • Williams P.J., and Allen M.S. The analysis of flavouring compounds in grapes. In: Linskens H.F., and Jackson J.F. (Eds). Modern Methods of Plant Analysis, Vol. 18. Fruit Analysis (1996), Springer-Verlag, Berlin & Heidelberg 37-57
    • (1996) Modern Methods of Plant Analysis, Vol. 18. Fruit Analysis , pp. 37-57
    • Williams, P.J.1    Allen, M.S.2
  • 184
    • 0000611658 scopus 로고
    • Chemical structure of anthocyanins
    • Markakis P. (Ed), Academic Press, New York
    • Brouillard R. Chemical structure of anthocyanins. In: Markakis P. (Ed). Anthocyanins as Food Colours (1982), Academic Press, New York XX
    • (1982) Anthocyanins as Food Colours
    • Brouillard, R.1
  • 185
    • 0025633123 scopus 로고
    • L-Ascorbic acid α-glucoside formed by regioselective transglucosylation with rat intestinal and rice seed α-glucosidases: Its improved stability and structure determination
    • Yamamoto I., Muto N., Murakami K., Suga S., and Yamaguchi H. L-Ascorbic acid α-glucoside formed by regioselective transglucosylation with rat intestinal and rice seed α-glucosidases: Its improved stability and structure determination. Chem. Pharm. Bull. 38 (1990) 3020-3023
    • (1990) Chem. Pharm. Bull. , vol.38 , pp. 3020-3023
    • Yamamoto, I.1    Muto, N.2    Murakami, K.3    Suga, S.4    Yamaguchi, H.5
  • 186
    • 0000545916 scopus 로고
    • Release and modification of nod-gene-inducing flavonoids from alfalfa seeds
    • Hartwig U.A., and Phillips D.A. Release and modification of nod-gene-inducing flavonoids from alfalfa seeds. Plant Physiol. 95 (1991) 804-807
    • (1991) Plant Physiol. , vol.95 , pp. 804-807
    • Hartwig, U.A.1    Phillips, D.A.2
  • 187
    • 0001493461 scopus 로고
    • Alfalfa (Medicago sativa L.) root exudates contain isoflavonoids in the presence of Rhizobium meliloti
    • Dakora F.D., Joseph C.M., and Phillips D.A. Alfalfa (Medicago sativa L.) root exudates contain isoflavonoids in the presence of Rhizobium meliloti. Plant Physiol. 101 (1993) 819-824
    • (1993) Plant Physiol. , vol.101 , pp. 819-824
    • Dakora, F.D.1    Joseph, C.M.2    Phillips, D.A.3
  • 188
    • 0003072628 scopus 로고
    • Hormone biosynthesis and metabolism: Auxin biosynthesis and metabolism
    • Davies P.J. (Ed), Kluwer Academic Publishers, Netherlands
    • Bandurski R.S., Cohen J.D., Slovin J.P., and Reinecke D.M. Hormone biosynthesis and metabolism: Auxin biosynthesis and metabolism. In: Davies P.J. (Ed). Plant Hormones (1995), Kluwer Academic Publishers, Netherlands 39-65
    • (1995) Plant Hormones , pp. 39-65
    • Bandurski, R.S.1    Cohen, J.D.2    Slovin, J.P.3    Reinecke, D.M.4
  • 190
    • 0000713887 scopus 로고
    • Transport of cyanogenic glucosides: linustatin uptake by Hevea cotyledons
    • Selmar D. Transport of cyanogenic glucosides: linustatin uptake by Hevea cotyledons. Planta 191 (1993) 191-199
    • (1993) Planta , vol.191 , pp. 191-199
    • Selmar, D.1
  • 191
    • 0001251234 scopus 로고
    • The plant hormone concept: Concentration, sensitivity and transport
    • Davies P.J. (Ed), Kluwer Academic Publishers, Netherlands
    • Davies P.J. The plant hormone concept: Concentration, sensitivity and transport. In: Davies P.J. (Ed). Plant Hormones (1995), Kluwer Academic Publishers, Netherlands 13-38
    • (1995) Plant Hormones , pp. 13-38
    • Davies, P.J.1
  • 192
    • 0030267948 scopus 로고    scopus 로고
    • Dhurrin-6′-glucoside, a cyanogenic diglucoside from Sorghum bicolor
    • Selmar D., Irandoost Z., and Wray V. Dhurrin-6′-glucoside, a cyanogenic diglucoside from Sorghum bicolor. Phytochemistry 43 (1996) 569-572
    • (1996) Phytochemistry , vol.43 , pp. 569-572
    • Selmar, D.1    Irandoost, Z.2    Wray, V.3
  • 193
    • 0029328449 scopus 로고
    • Flavonol 3-O-glycosyltransferase associated with petunia pollen produce gametophyte-specific flavonol diglycosides
    • Vogt T., and Taylor L.P. Flavonol 3-O-glycosyltransferase associated with petunia pollen produce gametophyte-specific flavonol diglycosides. Plant Physiol. 108 (1995) 903-911
    • (1995) Plant Physiol. , vol.108 , pp. 903-911
    • Vogt, T.1    Taylor, L.P.2
  • 194
    • 0017953125 scopus 로고
    • An enzymatic assay for the total cyanide content of cassava (Manihot esculenta Crantz)
    • Cooke R.D. An enzymatic assay for the total cyanide content of cassava (Manihot esculenta Crantz). J. Sci. Food Agric. 29 (1978) 345-352
    • (1978) J. Sci. Food Agric. , vol.29 , pp. 345-352
    • Cooke, R.D.1
  • 195
    • 0000806639 scopus 로고
    • The volatile composition of Chardonnay juices: A study by flavour precursor analysis
    • Sefton M.A., Francis I.L., and Williams P.J. The volatile composition of Chardonnay juices: A study by flavour precursor analysis. Amer. J. Enol. Viticult. 44 (1993) 359-370
    • (1993) Amer. J. Enol. Viticult. , vol.44 , pp. 359-370
    • Sefton, M.A.1    Francis, I.L.2    Williams, P.J.3
  • 196
    • 84985268190 scopus 로고
    • Free and bound volatile secondary metabolites of V. vinifera grape cv. Sauvignon Blanc
    • Sefton M.A., Francis I.L., and Williams P.J. Free and bound volatile secondary metabolites of V. vinifera grape cv. Sauvignon Blanc. J. Food Sci. 59 (1994) 142-147
    • (1994) J. Food Sci. , vol.59 , pp. 142-147
    • Sefton, M.A.1    Francis, I.L.2    Williams, P.J.3
  • 197
    • 0001661184 scopus 로고
    • UDP-glucose: cyanidin-3-O-glucosyltransferase from red cabbage seedlings
    • Saleh A.M., Poulton J.E., and Grisebach H. UDP-glucose: cyanidin-3-O-glucosyltransferase from red cabbage seedlings. Phytochemistry 15 (1976) 1865-1868
    • (1976) Phytochemistry , vol.15 , pp. 1865-1868
    • Saleh, A.M.1    Poulton, J.E.2    Grisebach, H.3
  • 198
    • 0020097027 scopus 로고
    • Isolation and partial characterization of three glucosyltransferase involved in the biosynthesis of flavonol triglucosides
    • Jourdan P.S., and Mansell R.L. Isolation and partial characterization of three glucosyltransferase involved in the biosynthesis of flavonol triglucosides. Arch. Biochem. Biophys. 213 (1982) 434-443
    • (1982) Arch. Biochem. Biophys. , vol.213 , pp. 434-443
    • Jourdan, P.S.1    Mansell, R.L.2
  • 199
    • 0001498601 scopus 로고
    • Purification and properties of a UDP glucose:flavonoid-3-O-glucosyltransferase from Hippeastrum petals
    • HRazdina G. Purification and properties of a UDP glucose:flavonoid-3-O-glucosyltransferase from Hippeastrum petals. Biochim. Biophys. Acta 955 (1988) 301-309
    • (1988) Biochim. Biophys. Acta , vol.955 , pp. 301-309
    • HRazdina, G.1
  • 200
    • 0027222146 scopus 로고
    • Purification and properties of UDP-glucose: thiohydroximate glucosyltransferase from Brassica napus L. seedlings
    • Reed D.W., Davin L., Jain J.C., Deluca V., Nelson L., and Underhill E.W. Purification and properties of UDP-glucose: thiohydroximate glucosyltransferase from Brassica napus L. seedlings. Arch. Biochem. Biophys. 305 (1993) 526-532
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 526-532
    • Reed, D.W.1    Davin, L.2    Jain, J.C.3    Deluca, V.4    Nelson, L.5    Underhill, E.W.6
  • 201
    • 0028002359 scopus 로고
    • The effects of heavy metals and root immersion on isoflavonoid metabolism in alfalfa (Medicago sativa L.)
    • Parry A.D., Tiller S.A., and Edwards R. The effects of heavy metals and root immersion on isoflavonoid metabolism in alfalfa (Medicago sativa L.). Plant Physiol. 106 (1994) 195-202
    • (1994) Plant Physiol. , vol.106 , pp. 195-202
    • Parry, A.D.1    Tiller, S.A.2    Edwards, R.3
  • 202
    • 0010442473 scopus 로고
    • Purification and partial characterization of UDP-glucose phenol-β-D-glucosyltransferase from papaya fruit
    • Keil U., and Schreier P. Purification and partial characterization of UDP-glucose phenol-β-D-glucosyltransferase from papaya fruit. Phytochemistry 27 (1989) 2281-2284
    • (1989) Phytochemistry , vol.27 , pp. 2281-2284
    • Keil, U.1    Schreier, P.2
  • 203
    • 0025950637 scopus 로고
    • Enzymic synthesis of 1-O-(indole-3-ylacetyl)-β-D-glucose
    • Kowalczyk S., and Bandurski R.S. Enzymic synthesis of 1-O-(indole-3-ylacetyl)-β-D-glucose. Biochem J. 269 (1991) 509-514
    • (1991) Biochem J. , vol.269 , pp. 509-514
    • Kowalczyk, S.1    Bandurski, R.S.2
  • 204
    • 0033199424 scopus 로고    scopus 로고
    • Cloning and expression of a cDNA encoding betanidin 5-O-glucosyltransferase, a betanidin- and flavonoid-specific enzyme with high homology to inducible glucosyltransferases from the Solanaceae
    • Vogt T., Grimm R., and Strack D. Cloning and expression of a cDNA encoding betanidin 5-O-glucosyltransferase, a betanidin- and flavonoid-specific enzyme with high homology to inducible glucosyltransferases from the Solanaceae. Plant J. 19 (1999) 509-519
    • (1999) Plant J. , vol.19 , pp. 509-519
    • Vogt, T.1    Grimm, R.2    Strack, D.3
  • 205
    • 0019638448 scopus 로고
    • UDP-glucose:isoflavone 7-O-glucosyltransferase from roots of chick pea (Cicer arietinum L.)
    • Köster J., and Barz W. UDP-glucose:isoflavone 7-O-glucosyltransferase from roots of chick pea (Cicer arietinum L.). Arch. Biochem. Biophys. 212 (1981) 98-104
    • (1981) Arch. Biochem. Biophys. , vol.212 , pp. 98-104
    • Köster, J.1    Barz, W.2
  • 206
    • 0000205351 scopus 로고
    • Properties and genetic control of anthocyanin 5-O-glucosyltransferase in flowers of Petunia hybrida
    • Jonsson L.M.V., Aarsman M.E.G., Van Diepen P., De Vlaming N., Smit N., and Schram A.W. Properties and genetic control of anthocyanin 5-O-glucosyltransferase in flowers of Petunia hybrida. Planta 160 (1984) 341-347
    • (1984) Planta , vol.160 , pp. 341-347
    • Jonsson, L.M.V.1    Aarsman, M.E.G.2    Van Diepen, P.3    De Vlaming, N.4    Smit, N.5    Schram, A.W.6
  • 207
    • 0010039261 scopus 로고
    • Detection and characterization of UDP-glucose:flavonoid O-glucosyltransferases in the leaves of Prunus x yedoensis Matsum
    • Ishikura N., and Yamamoto M. Detection and characterization of UDP-glucose:flavonoid O-glucosyltransferases in the leaves of Prunus x yedoensis Matsum. Plant Cell Physiol. 31 (1990) 1109-1115
    • (1990) Plant Cell Physiol. , vol.31 , pp. 1109-1115
    • Ishikura, N.1    Yamamoto, M.2
  • 208
    • 0025904183 scopus 로고
    • Plant biochemistry of xenobiotics: Isolation and properties of Soybean O- and N-glucosyl and O- and N-malonyltransferases for chlorinated phenols and anilines
    • Sandermann H., Schmitt R., Eckey H., and Bauknecht T. Plant biochemistry of xenobiotics: Isolation and properties of Soybean O- and N-glucosyl and O- and N-malonyltransferases for chlorinated phenols and anilines. Arch. Biochem. Biophys. 287 (1991) 341-350
    • (1991) Arch. Biochem. Biophys. , vol.287 , pp. 341-350
    • Sandermann, H.1    Schmitt, R.2    Eckey, H.3    Bauknecht, T.4
  • 209
    • 0000057676 scopus 로고
    • Partial purification and some properties of flavonol 3-O-glycosyltransferase from seedlings of Vigna mungo, with special reference to the formational of kaempferol 3-O-galactoside and 3-O0glucoside
    • Ishikura N., and Mato M. Partial purification and some properties of flavonol 3-O-glycosyltransferase from seedlings of Vigna mungo, with special reference to the formational of kaempferol 3-O-galactoside and 3-O0glucoside. Plant Cell Physiol. 34 (1993) 329-335
    • (1993) Plant Cell Physiol. , vol.34 , pp. 329-335
    • Ishikura, N.1    Mato, M.2
  • 210
    • 0028086645 scopus 로고
    • UDP-glucose:flavonoid O-glucosyltransferase from strawberry fruit
    • Cheng G.W., Malencik D.A., and Breen P.J. UDP-glucose:flavonoid O-glucosyltransferase from strawberry fruit. Phytochemistry 35 (1994) 1435-1439
    • (1994) Phytochemistry , vol.35 , pp. 1435-1439
    • Cheng, G.W.1    Malencik, D.A.2    Breen, P.J.3
  • 211
    • 0028042854 scopus 로고
    • Multiple forms of flavonol O-glucosyltransferases in young leaves of Euonymus alatus F. Ciliato-Dentatus
    • Ishikura N., and Yang Z.-Q. Multiple forms of flavonol O-glucosyltransferases in young leaves of Euonymus alatus F. Ciliato-Dentatus. Phytochemistry 36 (1994) 1139-1145
    • (1994) Phytochemistry , vol.36 , pp. 1139-1145
    • Ishikura, N.1    Yang, Z.-Q.2
  • 212
    • 0029199881 scopus 로고
    • Isolation and characterization of a UDP-glucose:cyanidin 3-O-glucosyltransferase from grape cell suspension cultures (V. vinifera L.)
    • Do C., Cormier F., and Nicolas Y. Isolation and characterization of a UDP-glucose:cyanidin 3-O-glucosyltransferase from grape cell suspension cultures (V. vinifera L.). Plant Sci. 112 (1995) 43-51
    • (1995) Plant Sci. , vol.112 , pp. 43-51
    • Do, C.1    Cormier, F.2    Nicolas, Y.3
  • 213
    • 0030062408 scopus 로고    scopus 로고
    • Purification and characterization of glycosyltransferases involved in anthocyanin biosynthesis in cell-suspension cultures of Daucus carota L
    • Rose A., Glabgen W.E., Hopp W., and Seitz H.U. Purification and characterization of glycosyltransferases involved in anthocyanin biosynthesis in cell-suspension cultures of Daucus carota L. Planta 198 (1996) 397-403
    • (1996) Planta , vol.198 , pp. 397-403
    • Rose, A.1    Glabgen, W.E.2    Hopp, W.3    Seitz, H.U.4
  • 214
    • 0010263191 scopus 로고
    • Isolation and characterization of a UDP-glucose:flavonol O-3-glucosyltransferase from illuminated red cabbage (Brassica oleracea cv red danish seedlings
    • Sun Y., and Hrazdina G. Isolation and characterization of a UDP-glucose:flavonol O-3-glucosyltransferase from illuminated red cabbage (Brassica oleracea cv red danish seedlings. Plant Physiol. 95 (1991) 570-576
    • (1991) Plant Physiol. , vol.95 , pp. 570-576
    • Sun, Y.1    Hrazdina, G.2
  • 215
    • 0000316591 scopus 로고
    • Cloning of the Bronze locus in maize by a simple and generalizable procedure using the transposable controlling element Activator (Ac.)
    • Fedoroff N.V., Furtek D.B., and Nelson O.E. Cloning of the Bronze locus in maize by a simple and generalizable procedure using the transposable controlling element Activator (Ac.). Proc. Natl. Acad. Sci. USA 71 (1984) 2825-3829
    • (1984) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 2825-3829
    • Fedoroff, N.V.1    Furtek, D.B.2    Nelson, O.E.3
  • 216
    • 0026192097 scopus 로고
    • Control of anthocyanin biosynthesis in flowers of Anthirrhinum majus
    • Martin C., Prescott A., Mackay S., Bartlett J., and Vrijlandt E. Control of anthocyanin biosynthesis in flowers of Anthirrhinum majus. Plant J. 1 (1991) 37-49
    • (1991) Plant J. , vol.1 , pp. 37-49
    • Martin, C.1    Prescott, A.2    Mackay, S.3    Bartlett, J.4    Vrijlandt, E.5
  • 217
    • 0028386531 scopus 로고
    • Cloning and molecular analysis of structural genes involved in flavonoid and stilbene biosynthesis in grape (V. vinifera L.)
    • Sparvoli F., Martin C., Scienza A., Gavazzi G., and Tonelli C. Cloning and molecular analysis of structural genes involved in flavonoid and stilbene biosynthesis in grape (V. vinifera L.). Plant Mol. Biol. 24 (1994) 743-755
    • (1994) Plant Mol. Biol. , vol.24 , pp. 743-755
    • Sparvoli, F.1    Martin, C.2    Scienza, A.3    Gavazzi, G.4    Tonelli, C.5
  • 218
    • 0025386677 scopus 로고
    • Nucleotide sequence of the Bronze-1 homologous gene from Hordeum vulgare
    • Wise R.P., Rohde W., and Salamini F. Nucleotide sequence of the Bronze-1 homologous gene from Hordeum vulgare. Plant Mol. Biol. 14 (1990) 277-279
    • (1990) Plant Mol. Biol. , vol.14 , pp. 277-279
    • Wise, R.P.1    Rohde, W.2    Salamini, F.3
  • 219
    • 0027674297 scopus 로고
    • cDNA cloning and characterisation of novel ripening-related mRNAs with altered patterns of accumulation in the ripening inhibitor (rin) tomato ripening mutant
    • Picton S., Gray J., Barton S., Abubakar U., Lowe A., and Grierson D. cDNA cloning and characterisation of novel ripening-related mRNAs with altered patterns of accumulation in the ripening inhibitor (rin) tomato ripening mutant. Plant Mol. Biol. 23 (1993) 193-207
    • (1993) Plant Mol. Biol. , vol.23 , pp. 193-207
    • Picton, S.1    Gray, J.2    Barton, S.3    Abubakar, U.4    Lowe, A.5    Grierson, D.6
  • 220
    • 0028133772 scopus 로고
    • Isolation and characterization of a cDNA clone corresponding to the Rt locus of Petunia hybrida
    • Brugliera P., Holton T.A., Stevenson T.W., Farcy E., Lu C.-Y., and Cornish E.C. Isolation and characterization of a cDNA clone corresponding to the Rt locus of Petunia hybrida. Plant J. 5 (1994) 81-92
    • (1994) Plant J. , vol.5 , pp. 81-92
    • Brugliera, P.1    Holton, T.A.2    Stevenson, T.W.3    Farcy, E.4    Lu, C.-Y.5    Cornish, E.C.6
  • 221
    • 0030185051 scopus 로고    scopus 로고
    • Novel anthocyanins produced in petals of genetically transformed Lisianthus
    • Markham K.R. Novel anthocyanins produced in petals of genetically transformed Lisianthus. Phytochemistry 42 (1996) 1035-1038
    • (1996) Phytochemistry , vol.42 , pp. 1035-1038
    • Markham, K.R.1
  • 222
    • 0028171620 scopus 로고
    • iaglu, a gene from Zea Mays involved in conjugation of growth hormone indole-3-acetic acid
    • Szerszen J., Szczyglowski K., and Bandurski R. iaglu, a gene from Zea Mays involved in conjugation of growth hormone indole-3-acetic acid. Science 265 (1994) 1699-1701
    • (1994) Science , vol.265 , pp. 1699-1701
    • Szerszen, J.1    Szczyglowski, K.2    Bandurski, R.3
  • 223
    • 0028312482 scopus 로고
    • Multiple secondary plant product UDP-glucose glucosyltransferase genes expressed in cassava (Manihot esculenta Crantz) cotyledons
    • Hughes J., and Hughes M.A. Multiple secondary plant product UDP-glucose glucosyltransferase genes expressed in cassava (Manihot esculenta Crantz) cotyledons. DNA Sequence 5 (1994) 41-49
    • (1994) DNA Sequence , vol.5 , pp. 41-49
    • Hughes, J.1    Hughes, M.A.2
  • 224
    • 0029108258 scopus 로고
    • Baculovirus-encoded ecdysteroid UDP-glucosyltransferases
    • O'Reilly D.R. Baculovirus-encoded ecdysteroid UDP-glucosyltransferases. Insect Biochem. Molec. Biol. 25 (1995) 541-550
    • (1995) Insect Biochem. Molec. Biol. , vol.25 , pp. 541-550
    • O'Reilly, D.R.1
  • 225
    • 0026644417 scopus 로고
    • Functional expression of a zeaxanthin glucosyltransferase from Erwinia herbicola and a proposed uridine diphosphate binding site
    • Hundle B.S., O'Brien D.A., Alberti M., Beyer P., and Hearst J.E. Functional expression of a zeaxanthin glucosyltransferase from Erwinia herbicola and a proposed uridine diphosphate binding site. Proc. Natl. Acad. Sci. USA 89 (1992) 9321-9325
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9321-9325
    • Hundle, B.S.1    O'Brien, D.A.2    Alberti, M.3    Beyer, P.4    Hearst, J.E.5
  • 226
    • 0025236448 scopus 로고
    • Expression of chimeric cDNAs in cell culture defines a region of UDP-glucuronosyltransferase involved in substrate selection
    • Mackenzie P.I. Expression of chimeric cDNAs 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
  • 227
    • 0026701911 scopus 로고
    • A novel complex locus UG1 encodes human bilirubin, phenol, and other UDP-glucoronosyltransferase isozymes with identical carboxyl termini
    • Ritter J.K., Chen F., Sheen Y.Y., Tran H.M., Kimura S., Yeatman M.T., and Owens I.S. A novel complex locus UG1 encodes human bilirubin, phenol, and other UDP-glucoronosyltransferase isozymes with identical carboxyl termini. J. Biol. Chem. 267 (1992) 3257-3261
    • (1992) J. Biol. Chem. , vol.267 , pp. 3257-3261
    • Ritter, J.K.1    Chen, F.2    Sheen, Y.Y.3    Tran, H.M.4    Kimura, S.5    Yeatman, M.T.6    Owens, I.S.7
  • 228
    • 84943107683 scopus 로고
    • Prunasin biosynthesis by cell-free extracts from black cherry (Prunus serotina Ehrh.) fruits and leaves
    • Poulton J.E., and Shin S.-I. Prunasin biosynthesis by cell-free extracts from black cherry (Prunus serotina Ehrh.) fruits and leaves. Z. Naturforsch 38c (1983) 369-374
    • (1983) Z. Naturforsch , vol.38 c , pp. 369-374
    • Poulton, J.E.1    Shin, S.-I.2
  • 229
    • 0042401271 scopus 로고
    • The biosynthesis of cyanogenic glucosides and glucosinolates
    • Dewick. The biosynthesis of cyanogenic glucosides and glucosinolates. Natural Prod. Rep. 1 (1984) 545-549
    • (1984) Natural Prod. Rep. , vol.1 , pp. 545-549
    • Dewick1
  • 230
    • 0001237403 scopus 로고
    • Sequence comparisons of three wild-type Bronze-1 alleles from Zea mays
    • Furtek D., Schielfbein J.W., Johnston F., and Nelson O.E. Sequence comparisons of three wild-type Bronze-1 alleles from Zea mays. Plant Mol. Biol. 11 (1988) 473-481
    • (1988) Plant Mol. Biol. , vol.11 , pp. 473-481
    • Furtek, D.1    Schielfbein, J.W.2    Johnston, F.3    Nelson, O.E.4
  • 231
    • 3543042687 scopus 로고
    • Localization of cinnamic acid 4-monooxygenase and the membrane-bound enzyme system for dhurrin biosynthesis in Sorghum seedlings
    • Saunders J.A., Conn E.E., Lin C.H., and Shimada M. Localization of cinnamic acid 4-monooxygenase and the membrane-bound enzyme system for dhurrin biosynthesis in Sorghum seedlings. Plant Physiol. 60 (1977) 629-634
    • (1977) Plant Physiol. , vol.60 , pp. 629-634
    • Saunders, J.A.1    Conn, E.E.2    Lin, C.H.3    Shimada, M.4
  • 232
    • 32644468599 scopus 로고
    • Cyanogenesis in Sorghum vulgare. II. Mechanism of the alkaline hydrolysis of dhurrin (p-hydroxymandelonitrile glucoside)
    • Mao C.H., and Anderson L. Cyanogenesis in Sorghum vulgare. II. Mechanism of the alkaline hydrolysis of dhurrin (p-hydroxymandelonitrile glucoside). J. Org. Chem. 30 (1965) 603-607
    • (1965) J. Org. Chem. , vol.30 , pp. 603-607
    • Mao, C.H.1    Anderson, L.2
  • 233
    • 0028190831 scopus 로고
    • Immunocytological localization of hydroxynitrile lyases from Sorghum bicolor L. and Linum usitatissimum L
    • Wajant H., Riedel D., Benz S., and Mundry K.W. Immunocytological localization of hydroxynitrile lyases from Sorghum bicolor L. and Linum usitatissimum L. Plant Sci. 103 (1994) 145-154
    • (1994) Plant Sci. , vol.103 , pp. 145-154
    • Wajant, H.1    Riedel, D.2    Benz, S.3    Mundry, K.W.4
  • 234
    • 0028795264 scopus 로고
    • Cyanogenesis in cassava (Manihot esculenta Crantz)
    • McMahon J.M., White W.L.B., and Sayre R.T. Cyanogenesis in cassava (Manihot esculenta Crantz). J. Exptl. Bot. 46 (1995) 731-741
    • (1995) J. Exptl. Bot. , vol.46 , pp. 731-741
    • McMahon, J.M.1    White, W.L.B.2    Sayre, R.T.3
  • 235
    • 0010286922 scopus 로고
    • Incorporation of hydrocyanic acid labelled with carbon-14 into asparagine in seedlings
    • Blumenthal-Goldschmidt S., Butler G.W., and Conn E.E. Incorporation of hydrocyanic acid labelled with carbon-14 into asparagine in seedlings. Nature 197 (1963) 718-719
    • (1963) Nature , vol.197 , pp. 718-719
    • Blumenthal-Goldschmidt, S.1    Butler, G.W.2    Conn, E.E.3
  • 236
    • 0019352220 scopus 로고
    • Die cyanogenen Glykoside von Triticum, Secale und Sorghum
    • Erb N., Zinsmeister H.D., and Nahrstedt A. Die cyanogenen Glykoside von Triticum, Secale und Sorghum. Planta Med. 41 (1981) 84-89
    • (1981) Planta Med. , vol.41 , pp. 84-89
    • Erb, N.1    Zinsmeister, H.D.2    Nahrstedt, A.3
  • 237
    • 0011352261 scopus 로고
    • Amount and distribution of hydrocyanic acid potential during the life cycle of plants of three sorghum cultivars
    • Loyd R.C., and Gray E. Amount and distribution of hydrocyanic acid potential during the life cycle of plants of three sorghum cultivars. Agr. J. 62 (1970) 394-397
    • (1970) Agr. J. , vol.62 , pp. 394-397
    • Loyd, R.C.1    Gray, E.2
  • 238
    • 0005094599 scopus 로고
    • Ultrastructural and developmental alterations induced by Periconia circinata toxin in the root tip of sorghum
    • Arias J.A., Dunkle L.D., and Bracker C.E. Ultrastructural and developmental alterations induced by Periconia circinata toxin in the root tip of sorghum. Can. J. Bot. 61 (1983) 1491-1505
    • (1983) Can. J. Bot. , vol.61 , pp. 1491-1505
    • Arias, J.A.1    Dunkle, L.D.2    Bracker, C.E.3
  • 239
    • 0002659904 scopus 로고
    • Pattern of the cyanide-potential in developing fruits
    • Frehner M., Scalet M., and Conn E.E. Pattern of the cyanide-potential in developing fruits. Plant Physiol. 94 (1990) 28-34
    • (1990) Plant Physiol. , vol.94 , pp. 28-34
    • Frehner, M.1    Scalet, M.2    Conn, E.E.3
  • 240
    • 0005362367 scopus 로고
    • Purification and properties of endosperm protoplasts of Hevea brasiliensis L
    • Selmar D., Frehner M., and Conn E.E. Purification and properties of endosperm protoplasts of Hevea brasiliensis L. J. Plant Physiol. 135 (1989) 105-109
    • (1989) J. Plant Physiol. , vol.135 , pp. 105-109
    • Selmar, D.1    Frehner, M.2    Conn, E.E.3
  • 241
    • 0023213217 scopus 로고
    • Characterization of β-glucosidases with high specificity for the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench seedlings
    • Hösel W., Tober I., Eklund S.H., and Conn E.E. Characterization of β-glucosidases with high specificity for the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench seedlings. Arch. Biochem. Biophys. 252 (1987) 152-162
    • (1987) Arch. Biochem. Biophys. , vol.252 , pp. 152-162
    • Hösel, W.1    Tober, I.2    Eklund, S.H.3    Conn, E.E.4
  • 242
    • 0000297833 scopus 로고
    • Tissue distributions of dhurrin and of enzymes involved in its metabolism in leaves of Sorghum bicolor
    • Kojima M., Poulton J.E., Thayer S.S., and Conn E.E. Tissue distributions of dhurrin and of enzymes involved in its metabolism in leaves of Sorghum bicolor. Plant Physiol. 63 (1979) 1022-1028
    • (1979) Plant Physiol. , vol.63 , pp. 1022-1028
    • Kojima, M.1    Poulton, J.E.2    Thayer, S.S.3    Conn, E.E.4
  • 243
    • 0000403124 scopus 로고
    • The linamarin α-glucosidase in Costa Rican wild lima beans (Phaseolus lunatus L.) is apoplastic
    • Frehner M., and Conn E.E. The linamarin α-glucosidase in Costa Rican wild lima beans (Phaseolus lunatus L.) is apoplastic. Plant Physiol. 84 (1987) 1296-1300
    • (1987) Plant Physiol. , vol.84 , pp. 1296-1300
    • Frehner, M.1    Conn, E.E.2
  • 244
    • 0000225005 scopus 로고
    • Linamarase and other β-glucosidases are present in the cell walls of Trifolium repens L. leaves
    • Kakes P. Linamarase and other β-glucosidases are present in the cell walls of Trifolium repens L. leaves. Planta 166 (1985) 156-160
    • (1985) Planta , vol.166 , pp. 156-160
    • Kakes, P.1
  • 245
    • 77957763336 scopus 로고
    • Linustatin, the linamarin-glucoside protected against cleavage by apoplastic linamarase
    • Kurzhals C.H., Grützmacher H., Selmar D., and Biehl B. Linustatin, the linamarin-glucoside protected against cleavage by apoplastic linamarase. Planta Medica 55 (1989) 673
    • (1989) Planta Medica , vol.55 , pp. 673
    • Kurzhals, C.H.1    Grützmacher, H.2    Selmar, D.3    Biehl, B.4
  • 246
    • 0030065775 scopus 로고    scopus 로고
    • Copurification from E. coli of a plant beta-glucosidase-glutathione S-transferase fusion protein and the bacterial chaperonin GroEL
    • Keresztessy Z., Hughes J., Kiss L., and Hughes M.A. Copurification from E. coli of a plant beta-glucosidase-glutathione S-transferase fusion protein and the bacterial chaperonin GroEL. Biochem. J. 314 (1996) 41-47
    • (1996) Biochem. J. , vol.314 , pp. 41-47
    • Keresztessy, Z.1    Hughes, J.2    Kiss, L.3    Hughes, M.A.4
  • 248
    • 0032695916 scopus 로고    scopus 로고
    • Evidence for enzyme complexes in the phenylpropanoid and flavonoid pathways
    • Winkel-Shirley B. Evidence for enzyme complexes in the phenylpropanoid and flavonoid pathways. Physiol. Plant. 107 (1999) 142-149
    • (1999) Physiol. Plant. , vol.107 , pp. 142-149
    • Winkel-Shirley, B.1
  • 249
    • 77957794957 scopus 로고    scopus 로고
    • Metabolic engineering of p-hydroxybenzylglucosinolate in Arabidopsis by expression of the cyanogenic CYP79A1 from Sorghum bicolor
    • in press
    • in press. Bak S., Olsen C.E., Møller B.L., and Halkier B.A. Metabolic engineering of p-hydroxybenzylglucosinolate in Arabidopsis by expression of the cyanogenic CYP79A1 from Sorghum bicolor. Plant J. (2000)
    • (2000) Plant J.
    • Bak, S.1    Olsen, C.E.2    Møller, B.L.3    Halkier, B.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.