메뉴 건너뛰기




Volumn 52, Issue C, 2009, Pages 87-113

Chapter 4 Roles of γ-Glutamyl Transpeptidase and γ-Glutamyl Cyclotransferase in Glutathione and Glutathione-Conjugate Metabolism in Plants

Author keywords

[No Author keywords available]

Indexed keywords


EID: 71549123702     PISSN: 00652296     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-2296(10)52004-4     Document Type: Review
Times cited : (14)

References (86)
  • 1
    • 33846965940 scopus 로고    scopus 로고
    • Autoprocessing of Helicobacter pylori γ-glutamyl transpeptidase leads to the formation of a threonine-threonine catalytic triad
    • Boanca G., Sand A., Okada T., Suzuki H., Kumagai H., Fukuyama K., and Barycki J.J. Autoprocessing of Helicobacter pylori γ-glutamyl transpeptidase leads to the formation of a threonine-threonine catalytic triad. Journal of Biological Chemistry 282 (2007) 534-541
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 534-541
    • Boanca, G.1    Sand, A.2    Okada, T.3    Suzuki, H.4    Kumagai, H.5    Fukuyama, K.6    Barycki, J.J.7
  • 3
    • 33745647317 scopus 로고    scopus 로고
    • Maturation of Arabidopsis seeds is dependent on glutathione biosynthesis within the embryo
    • Cairns N.G., Pasternak M., Wachter A., Cobbett C.S., and Meyer A.J. Maturation of Arabidopsis seeds is dependent on glutathione biosynthesis within the embryo. Plant Physiology 141 (2006) 446-455
    • (2006) Plant Physiology , vol.141 , pp. 446-455
    • Cairns, N.G.1    Pasternak, M.2    Wachter, A.3    Cobbett, C.S.4    Meyer, A.J.5
  • 4
    • 0037002169 scopus 로고    scopus 로고
    • Phytochelatins and metallothioneins: roles in heavy metal detoxification and homeostasis
    • Cobbett C., and Goldsbrough P. Phytochelatins and metallothioneins: roles in heavy metal detoxification and homeostasis. Annual Review of Plant Biology 53 (2002) 159-182
    • (2002) Annual Review of Plant Biology , vol.53 , pp. 159-182
    • Cobbett, C.1    Goldsbrough, P.2
  • 5
    • 0031127932 scopus 로고    scopus 로고
    • Detoxification of xenobiotics by plants: Chemical modification and vacuolar compartmentation
    • Coleman J., Blake-Kalff M., and Davies E. Detoxification of xenobiotics by plants: Chemical modification and vacuolar compartmentation. Trends in Plant Science 2 (1997) 144-151
    • (1997) Trends in Plant Science , vol.2 , pp. 144-151
    • Coleman, J.1    Blake-Kalff, M.2    Davies, E.3
  • 6
    • 0028858946 scopus 로고
    • Properties of a maize glutathione S-transferase that conjugates coumaric acid and other phenylpropanoids
    • Dean J.V., Devarenne T.P., Lee I.S., and Orlofsky L.E. Properties of a maize glutathione S-transferase that conjugates coumaric acid and other phenylpropanoids. Plant Physiology 108 (1995) 985-994
    • (1995) Plant Physiology , vol.108 , pp. 985-994
    • Dean, J.V.1    Devarenne, T.P.2    Lee, I.S.3    Orlofsky, L.E.4
  • 7
    • 41149118605 scopus 로고    scopus 로고
    • Solution structure of At3g28950 from Arabidopsis thaliana
    • de la Cruz N.B., Peterson F.C., and Volkman B.F. Solution structure of At3g28950 from Arabidopsis thaliana. Proteins 71 (2008) 546-551
    • (2008) Proteins , vol.71 , pp. 546-551
    • de la Cruz, N.B.1    Peterson, F.C.2    Volkman, B.F.3
  • 10
    • 0034192572 scopus 로고    scopus 로고
    • Plant glutathione S-transferases: Enzymes with multiple functions in sickness and in health
    • Edwards R., Dixon D.P., and Walbot V. Plant glutathione S-transferases: Enzymes with multiple functions in sickness and in health. Trends in Plant Science 5 (2000) 193-198
    • (2000) Trends in Plant Science , vol.5 , pp. 193-198
    • Edwards, R.1    Dixon, D.P.2    Walbot, V.3
  • 11
    • 57449092576 scopus 로고    scopus 로고
    • Glutamyl transferase in the cell wall participates in extracellular glutathione salvage from the root apoplast
    • Ferretti M., Destro T., Tosatto S.C.E., La Rocca N., Rascio N., and Masi A. Glutamyl transferase in the cell wall participates in extracellular glutathione salvage from the root apoplast. New Phytologist 181 (2009) 115-126
    • (2009) New Phytologist , vol.181 , pp. 115-126
    • Ferretti, M.1    Destro, T.2    Tosatto, S.C.E.3    La Rocca, N.4    Rascio, N.5    Masi, A.6
  • 12
    • 25844468618 scopus 로고    scopus 로고
    • Redox homeostasis and antioxidant signaling: A metabolic interface between stress perception and physiological responses
    • Foyer C.H., and Noctor G. Redox homeostasis and antioxidant signaling: A metabolic interface between stress perception and physiological responses. The Plant Cell 17 (2005) 1866-1875
    • (2005) The Plant Cell , vol.17 , pp. 1866-1875
    • Foyer, C.H.1    Noctor, G.2
  • 13
    • 60749136076 scopus 로고    scopus 로고
    • Redox regulation in photosynthetic organisms: Signaling, acclimation, and practical implications
    • Foyer C.H., and Noctor G. Redox regulation in photosynthetic organisms: Signaling, acclimation, and practical implications. Antioxidants and Redox Signaling 11 (2009) 861-905
    • (2009) Antioxidants and Redox Signaling , vol.11 , pp. 861-905
    • Foyer, C.H.1    Noctor, G.2
  • 15
    • 0015244954 scopus 로고
    • Serum-glutamyl transpeptidase deficiency
    • Goodman S.I., Mace J.W., and Pollack S. Serum-glutamyl transpeptidase deficiency. The Lancet 1 (1971) 234-235
    • (1971) The Lancet , vol.1 , pp. 234-235
    • Goodman, S.I.1    Mace, J.W.2    Pollack, S.3
  • 16
    • 44849098699 scopus 로고    scopus 로고
    • The redox switch of γ-glutamylcysteine ligase via a reversible monomer-dimer transition is a mechanism unique to plants
    • Gromes R., Hothorn M., Lenherr E.D., Rybin V., Scheffzek K., and Rausch T. The redox switch of γ-glutamylcysteine ligase via a reversible monomer-dimer transition is a mechanism unique to plants. The Plant Journal 54 (2008) 1063-1075
    • (2008) The Plant Journal , vol.54 , pp. 1063-1075
    • Gromes, R.1    Hothorn, M.2    Lenherr, E.D.3    Rybin, V.4    Scheffzek, K.5    Rausch, T.6
  • 17
    • 34250798528 scopus 로고    scopus 로고
    • Glutamyl transpeptidase GGT4 initiates vacuolar degradation of glutathione S-conjugates in Arabidopsis
    • Grzam A., Martin M.N., Hell R., and Meyer A.J. Glutamyl transpeptidase GGT4 initiates vacuolar degradation of glutathione S-conjugates in Arabidopsis. FEBS Letters 581 (2007) 3131-3138
    • (2007) FEBS Letters , vol.581 , pp. 3131-3138
    • Grzam, A.1    Martin, M.N.2    Hell, R.3    Meyer, A.J.4
  • 19
    • 0021998639 scopus 로고
    • γ-Glutamyl transpeptidase-Its role in hepatocarcinogenesis
    • Hanigan M.H., and Pitot H.C. γ-Glutamyl transpeptidase-Its role in hepatocarcinogenesis. Carcinogenesis 6 (1985) 165-172
    • (1985) Carcinogenesis , vol.6 , pp. 165-172
    • Hanigan, M.H.1    Pitot, H.C.2
  • 20
    • 0030977130 scopus 로고    scopus 로고
    • Mice with genetic γ-glutamyl transpeptidase deficiency exhibit glutathionuria, severe growth failure, reduced life spans, and infertility
    • Harding C.O., Williams P., Wagner E., Chang D.S., Wild K., Colwell R.E., and Wolff J.A. Mice with genetic γ-glutamyl transpeptidase deficiency exhibit glutathionuria, severe growth failure, reduced life spans, and infertility. Journal of Biological Chemistry 272 (1997) 12560-12567
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 12560-12567
    • Harding, C.O.1    Williams, P.2    Wagner, E.3    Chang, D.S.4    Wild, K.5    Colwell, R.E.6    Wolff, J.A.7
  • 21
    • 34249963321 scopus 로고
    • γ-Glutamylcysteine synthetase in higher plants: Catalytic properties and subcellular localization
    • Hell R., and Bergmann L. γ-Glutamylcysteine synthetase in higher plants: Catalytic properties and subcellular localization. Planta 180 (1990) 603-612
    • (1990) Planta , vol.180 , pp. 603-612
    • Hell, R.1    Bergmann, L.2
  • 23
    • 0027467423 scopus 로고
    • Significance of Arg-107 and Glu-108 in the catalytic mechanism of human γ-glutamyl transpeptidase: Identification by site-directed mutagenesis
    • Ikeda Y., Fujii J., and Taniguchi N. Significance of Arg-107 and Glu-108 in the catalytic mechanism of human γ-glutamyl transpeptidase: Identification by site-directed mutagenesis. Journal of Biological Chemistry 268 (1993) 3980-3985
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 3980-3985
    • Ikeda, Y.1    Fujii, J.2    Taniguchi, N.3
  • 25
    • 0028977997 scopus 로고
    • Human γ-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residues of the light subunit
    • Ikeda Y., Fujii J., Taniguchi N., and Meister A. Human γ-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residues of the light subunit. Journal of Biological Chemistry 270 (1995) 12471-12475
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 12471-12475
    • Ikeda, Y.1    Fujii, J.2    Taniguchi, N.3    Meister, A.4
  • 26
    • 4043059910 scopus 로고    scopus 로고
    • Arabidopsis thaliana glutamate-cysteine ligase: Functional properties, kinetic mechanism, and regulation of activity
    • Jez J.M., Cahoon R.E., and Chen S. Arabidopsis thaliana glutamate-cysteine ligase: Functional properties, kinetic mechanism, and regulation of activity. Journal of Biological Chemistry 279 (2004) 33463-33470
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 33463-33470
    • Jez, J.M.1    Cahoon, R.E.2    Chen, S.3
  • 27
    • 0001236064 scopus 로고
    • Glutamyltranspeptidases in the metabolism of γ-glutamyl peptides in plants
    • Kasai T., Ohmiya A., and Sakamura S. Glutamyltranspeptidases in the metabolism of γ-glutamyl peptides in plants. Phytochemistry 21 (1982) 1233-1239
    • (1982) Phytochemistry , vol.21 , pp. 1233-1239
    • Kasai, T.1    Ohmiya, A.2    Sakamura, S.3
  • 28
    • 4243223278 scopus 로고
    • Occurrence and some properties of the novel γ-glutamyl transferase responsible for the synthesis of γ-l-glutamyl-d-alanine in pea seedlings
    • Kawasaki Y., Ogawa T., and Sasaoka K. Occurrence and some properties of the novel γ-glutamyl transferase responsible for the synthesis of γ-l-glutamyl-d-alanine in pea seedlings. Biochimica et Biophysica Acta 716 (1982) 194-200
    • (1982) Biochimica et Biophysica Acta , vol.716 , pp. 194-200
    • Kawasaki, Y.1    Ogawa, T.2    Sasaoka, K.3
  • 29
    • 30144433165 scopus 로고    scopus 로고
    • γ-Glutamyltranspeptidase: Disulfide bridges, propeptide cleavage, and activation in the endoplasmic reticulum
    • Kinlough C.L., Poland P.A., Bruns J.B., and Hughey R.P. γ-Glutamyltranspeptidase: Disulfide bridges, propeptide cleavage, and activation in the endoplasmic reticulum. Methods in Enzymology 401 (2005) 426-449
    • (2005) Methods in Enzymology , vol.401 , pp. 426-449
    • Kinlough, C.L.1    Poland, P.A.2    Bruns, J.B.3    Hughey, R.P.4
  • 30
    • 37649000618 scopus 로고    scopus 로고
    • Purification and characterization of dipeptidase hydrolyzing l-cysteinylglycine from radish cotyledon
    • Kumada H.-O., Koizumi Y., and Sekiya J. Purification and characterization of dipeptidase hydrolyzing l-cysteinylglycine from radish cotyledon. Bioscience, Biotechnology and Biochemistry 71 (2007) 3102-3104
    • (2007) Bioscience, Biotechnology and Biochemistry , vol.71 , pp. 3102-3104
    • Kumada, H.-O.1    Koizumi, Y.2    Sekiya, J.3
  • 34
    • 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
  • 36
    • 0030042346 scopus 로고    scopus 로고
    • Antioxidants in the apoplast and symplast of beech (Fagus sylvatica L.) leaves: Seasonal variations and responses to changing ozone concentrations in air
    • Luwe M. Antioxidants in the apoplast and symplast of beech (Fagus sylvatica L.) leaves: Seasonal variations and responses to changing ozone concentrations in air. Plant Cell and Environment 19 (1996) 321-328
    • (1996) Plant Cell and Environment , vol.19 , pp. 321-328
    • Luwe, M.1
  • 38
    • 0029009655 scopus 로고
    • A glutathione S-transferase involved in vacuolar transfer encoded by the maize gene Broneze-2
    • Marrs K.A., Alfenito M.R., Lloyd A.M., and Walbot V. A glutathione S-transferase involved in vacuolar transfer encoded by the maize gene Broneze-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    Walbot, V.4
  • 39
    • 0034004987 scopus 로고    scopus 로고
    • Purified γ-glutamyl transpeptidases from tomato exhibit high affinity for glutathione and glutathione S-conjugates
    • Martin M.N., and Slovin J.P. Purified γ-glutamyl transpeptidases from tomato exhibit high affinity for glutathione and glutathione S-conjugates. Plant Physiology 122 (2000) 1417-1426
    • (2000) Plant Physiology , vol.122 , pp. 1417-1426
    • Martin, M.N.1    Slovin, J.P.2
  • 40
    • 34547885780 scopus 로고    scopus 로고
    • Localization of members of the γ-glutamyl transpeptidase family identifies sites of glutathione and glutathione S-conjugate hydrolysis
    • Martin M.N., Saladores P.H., Lambert E., Hudson A.O., and Leustek T. Localization of members of the γ-glutamyl transpeptidase family identifies sites of glutathione and glutathione S-conjugate hydrolysis. Plant Physiology 144 (2007) 1715-1732
    • (2007) Plant Physiology , vol.144 , pp. 1715-1732
    • Martin, M.N.1    Saladores, P.H.2    Lambert, E.3    Hudson, A.O.4    Leustek, T.5
  • 42
    • 0028170738 scopus 로고
    • Arabidopsis thaliana γ-glutamylcysteine synthetase is structurally unrelated to mammalian, yeast, and Escherichia coli homologs
    • May M.J., and Leaver C.J. Arabidopsis thaliana γ-glutamylcysteine synthetase is structurally unrelated to mammalian, yeast, and Escherichia coli homologs. Proceedings of the National Academy of Sciences of the United States of America 91 (1994) 10059-10063
    • (1994) Proceedings of the National Academy of Sciences of the United States of America , vol.91 , pp. 10059-10063
    • May, M.J.1    Leaver, C.J.2
  • 43
    • 0015915903 scopus 로고
    • On the enzymology of amino acid transport
    • Meister A. On the enzymology of amino acid transport. Science 180 (1973) 33-39
    • (1973) Science , vol.180 , pp. 33-39
    • Meister, A.1
  • 44
    • 0002684621 scopus 로고
    • Glutathione synthetase deficiency and other disorders of the γ-glutamyl cycle
    • Scriver C.R., Beaudet A.L., Sly W.S., and Valle D. (Eds), McGraw-Hill, New York
    • Meister A., and Larsson A. Glutathione synthetase deficiency and other disorders of the γ-glutamyl cycle. In: Scriver C.R., Beaudet A.L., Sly W.S., and Valle D. (Eds). The Metabolic and Molecular Bases of Inherited Disease Vol. 1 (1995), McGraw-Hill, New York 1461-1495
    • (1995) The Metabolic and Molecular Bases of Inherited Disease , vol.1 , pp. 1461-1495
    • Meister, A.1    Larsson, A.2
  • 46
    • 33749387659 scopus 로고    scopus 로고
    • Cloning and molecular analysis of radish (Raphanus sativus L.) cDNAs encoding heterodimeric γ-glutamyltransferase
    • Nakano Y., Prieto R., Hara M., and Sekiya J. Cloning and molecular analysis of radish (Raphanus sativus L.) cDNAs encoding heterodimeric γ-glutamyltransferase. Plant Biotechnology 23 (2006) 419-424
    • (2006) Plant Biotechnology , vol.23 , pp. 419-424
    • Nakano, Y.1    Prieto, R.2    Hara, M.3    Sekiya, J.4
  • 48
    • 33746464872 scopus 로고    scopus 로고
    • Subcellular localization and possible functions of γ-glutamyltransferase in the radish (Raphanus sativus L.) plant
    • Nakano Y., Okawa S., Prieto R., and Sekiya J. Subcellular localization and possible functions of γ-glutamyltransferase in the radish (Raphanus sativus L.) plant. Bioscience Biotechnology and Biochemistry 70 (2006) 1790-1793
    • (2006) Bioscience Biotechnology and Biochemistry , vol.70 , pp. 1790-1793
    • Nakano, Y.1    Okawa, S.2    Prieto, R.3    Sekiya, J.4
  • 50
    • 52049115466 scopus 로고    scopus 로고
    • The identification and structural characterization of C7orf24 as γ-glutamyl cyclotransferase. An essential enzyme in the γ-glutamyl cycle
    • Oakley A.J., Yamada T., Liu D., Coggan M., Clark A.G., and Board P.G. The identification and structural characterization of C7orf24 as γ-glutamyl cyclotransferase. An essential enzyme in the γ-glutamyl cycle. Journal of Biological Chemistry 283 (2008) 22031-22042
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 22031-22042
    • Oakley, A.J.1    Yamada, T.2    Liu, D.3    Coggan, M.4    Clark, A.G.5    Board, P.G.6
  • 51
    • 0000059899 scopus 로고
    • An abnormal sulphydryl compound in urine
    • O'Daly S. An abnormal sulphydryl compound in urine. Irish Journal of Medical Science 7 (1968) 578-579
    • (1968) Irish Journal of Medical Science , vol.7 , pp. 578-579
    • O'Daly, S.1
  • 53
    • 33847169054 scopus 로고    scopus 로고
    • Glutathione conjugates in the vacuole are degraded by γ-glutamyl transpeptidase GGT3 in Arabidopsis
    • Ohkama-Ohtsu N., Zhao P., Xiang C., and Oliver D.J. Glutathione conjugates in the vacuole are degraded by γ-glutamyl transpeptidase GGT3 in Arabidopsis. The Plant Journal 49 (2007) 878-888
    • (2007) The Plant Journal , vol.49 , pp. 878-888
    • Ohkama-Ohtsu, N.1    Zhao, P.2    Xiang, C.3    Oliver, D.J.4
  • 54
    • 57749107460 scopus 로고    scopus 로고
    • A γ-glutamyl transpeptidase-independent pathway of glutathione catabolism to glutamate via 5-oxoproline in Arabidopsis
    • Ohkama-Ohtsu N., Oikawa A., Zhao P., Xiang C., Saito K., and Oliver D.J. A γ-glutamyl transpeptidase-independent pathway of glutathione catabolism to glutamate via 5-oxoproline in Arabidopsis. Plant Physiology 148 (2008) 1603-1613
    • (2008) Plant Physiology , vol.148 , pp. 1603-1613
    • Ohkama-Ohtsu, N.1    Oikawa, A.2    Zhao, P.3    Xiang, C.4    Saito, K.5    Oliver, D.J.6
  • 55
    • 0034495297 scopus 로고    scopus 로고
    • Structural comparison of Ntn-hydrolases
    • Oinonen C., and Rouvinen J. Structural comparison of Ntn-hydrolases. Protein Science 9 (2000) 2329-2337
    • (2000) Protein Science , vol.9 , pp. 2329-2337
    • Oinonen, C.1    Rouvinen, J.2
  • 57
    • 34047276293 scopus 로고    scopus 로고
    • Crystal structure of the γ-glutamyltranspeptidase precursor protein from Escherichia coli: Structural changes upon autocatalytic processing and implications for the maturation mechanism
    • Okada T., Suzuki H., Wada K., Kumagai H., and Fukuyama K. Crystal structure of the γ-glutamyltranspeptidase precursor protein from Escherichia coli: Structural changes upon autocatalytic processing and implications for the maturation mechanism. Journal of Biological Chemistry 282 (2007) 2433-2439
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 2433-2439
    • Okada, T.1    Suzuki, H.2    Wada, K.3    Kumagai, H.4    Fukuyama, K.5
  • 58
    • 40549143429 scopus 로고    scopus 로고
    • Restricting glutathione biosynthesis to the cytosol is sufficient for normal plant development
    • Pasternak M., Lim B., Wirtz M., Hell R., Cobbett C.S., and Meyer A.J. Restricting glutathione biosynthesis to the cytosol is sufficient for normal plant development. The Plant Journal 53 (2008) 999-1012
    • (2008) The Plant Journal , vol.53 , pp. 999-1012
    • Pasternak, M.1    Lim, B.2    Wirtz, M.3    Hell, R.4    Cobbett, C.S.5    Meyer, A.J.6
  • 59
    • 0041569774 scopus 로고    scopus 로고
    • Apoplastic ascorbate metabolism and its role in the regulation of cell signaling
    • Pignocchi C., and Foyer C.H. Apoplastic ascorbate metabolism and its role in the regulation of cell signaling. Current Opinion in Plant Biology 6 (2003) 379-389
    • (2003) Current Opinion in Plant Biology , vol.6 , pp. 379-389
    • Pignocchi, C.1    Foyer, C.H.2
  • 60
    • 0033047445 scopus 로고    scopus 로고
    • MRP subfamily ABC transporters from plants and yeast
    • Rea P.A. MRP subfamily ABC transporters from plants and yeast. Journal of Experimental Botany 50 (1999) 895-913
    • (1999) Journal of Experimental Botany , vol.50 , pp. 895-913
    • Rea, P.A.1
  • 62
    • 0002532027 scopus 로고
    • Physiological processes that modulate the concentration of glutathione in plant cells
    • Rennenberg H., Brunold C., De Kok L.J., and Stulen I. (Eds), SPB Academic Publishing, The Hague, The Netherlands
    • Rennenberg H., and Lamoureux G.L. Physiological processes that modulate the concentration of glutathione in plant cells. In: Rennenberg H., Brunold C., De Kok L.J., and Stulen I. (Eds). Sulfur Nutrition and Assimilation in Higher Plants (1990), SPB Academic Publishing, The Hague, The Netherlands 53-65
    • (1990) Sulfur Nutrition and Assimilation in Higher Plants , pp. 53-65
    • Rennenberg, H.1    Lamoureux, G.L.2
  • 63
  • 64
    • 84989739215 scopus 로고
    • 5-oxoprolinase in Nicotiana tabacum: Catalytic properties and subcellular localization
    • Rennenberg H., Steinkamp R., and Kesselmeier J. 5-oxoprolinase in Nicotiana tabacum: Catalytic properties and subcellular localization. Physiologia Plantarum 62 (1981) 211-216
    • (1981) Physiologia Plantarum , vol.62 , pp. 211-216
    • Rennenberg, H.1    Steinkamp, R.2    Kesselmeier, J.3
  • 65
    • 4244167028 scopus 로고    scopus 로고
    • Patients with genetic defects in the γ-glutamyl cycle
    • Ristoff E., and Larsson A. Patients with genetic defects in the γ-glutamyl cycle. Chemico-Biological Interactions 111-112 (1998) 113-121
    • (1998) Chemico-Biological Interactions , vol.111-112 , pp. 113-121
    • Ristoff, E.1    Larsson, A.2
  • 66
    • 42949085825 scopus 로고    scopus 로고
    • The role of glutathione in photosynthetic organisms: Emerging functions for glutaredoxins and glutathionylation
    • Rouhier N., Lemaire S.D., and Jacquot J.-P. The role of glutathione in photosynthetic organisms: Emerging functions for glutaredoxins and glutathionylation. Annual Review of Plant Biology 59 (2008) 143-166
    • (2008) Annual Review of Plant Biology , vol.59 , pp. 143-166
    • Rouhier, N.1    Lemaire, S.D.2    Jacquot, J.-P.3
  • 67
    • 13844276844 scopus 로고    scopus 로고
    • Purification and cloning of a γ-glutamyl transpeptidase from onion (Allium cepa)
    • Shaw M.L., Pither-Joyce M.D., and McCallum J.A. Purification and cloning of a γ-glutamyl transpeptidase from onion (Allium cepa). Phytochemistry 66 (2005) 515-522
    • (2005) Phytochemistry , vol.66 , pp. 515-522
    • Shaw, M.L.1    Pither-Joyce, M.D.2    McCallum, J.A.3
  • 68
    • 84989736302 scopus 로고
    • γ-Glutamyl-transpeptidase in tobacco suspension cultures: Catalytic properties and subcellular localization
    • Steinkamp R., and Rennenberg H. γ-Glutamyl-transpeptidase in tobacco suspension cultures: Catalytic properties and subcellular localization. Physiologia Plantarum 61 (1984) 251-256
    • (1984) Physiologia Plantarum , vol.61 , pp. 251-256
    • Steinkamp, R.1    Rennenberg, H.2
  • 69
    • 0002673987 scopus 로고
    • Degradation of glutathione in plant cells: Evidence against the participation of a γ-glutamyl transpeptidase
    • Steinkamp R., and Rennenberg H. Degradation of glutathione in plant cells: Evidence against the participation of a γ-glutamyl transpeptidase. Zeitschrift für Naturforschung. Section C: Biosciences 40c (1985) 29-33
    • (1985) Zeitschrift für Naturforschung. Section C: Biosciences , vol.40 c , pp. 29-33
    • Steinkamp, R.1    Rennenberg, H.2
  • 70
    • 84989710127 scopus 로고
    • γ-Glutamylcyclotransferase in tobacco suspension cultures: Catalytic properties and subcellular localization
    • Steinkamp R., and Rennenberg H. γ-Glutamylcyclotransferase in tobacco suspension cultures: Catalytic properties and subcellular localization. Physiologia Plantarum 69 (1987) 499-503
    • (1987) Physiologia Plantarum , vol.69 , pp. 499-503
    • Steinkamp, R.1    Rennenberg, H.2
  • 72
    • 0037044805 scopus 로고    scopus 로고
    • Autocatalytic processing of γ-glutamyltranspeptidase
    • Suzuki H., and Kumagai H. Autocatalytic processing of γ-glutamyltranspeptidase. Journal of Biological Chemistry 277 (2002) 43536-43543
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 43536-43543
    • Suzuki, H.1    Kumagai, H.2
  • 73
    • 0022908614 scopus 로고
    • γ-Glutamyltranspeptidase from Escherichia coli K-12: Formation and localization
    • Suzuki H., Kumagai H., and Tockikura T. γ-Glutamyltranspeptidase from Escherichia coli K-12: Formation and localization. Journal of Bacteriology 168 (1986) 1332-1335
    • (1986) Journal of Bacteriology , vol.168 , pp. 1332-1335
    • Suzuki, H.1    Kumagai, H.2    Tockikura, T.3
  • 74
    • 33847173562 scopus 로고    scopus 로고
    • γ-Glutamyl transpeptidase
    • Barrett A., Rawlings N., and Woessner J. (Eds), Academic Press, London
    • Taniguchi N., and Ikeda Y. γ-Glutamyl transpeptidase. In: Barrett A., Rawlings N., and Woessner J. (Eds). Handbook of Proteolytic Enzymes (1998), Academic Press, London 512-516
    • (1998) Handbook of Proteolytic Enzymes , pp. 512-516
    • Taniguchi, N.1    Ikeda, Y.2
  • 75
    • 0022272470 scopus 로고
    • γ-Glutamyl transpeptidase from kidney
    • Tate S.S., and Meister A. γ-Glutamyl transpeptidase from kidney. Methods in Enzymology 113 (1985) 400-419
    • (1985) Methods in Enzymology , vol.113 , pp. 400-419
    • Tate, S.S.1    Meister, A.2
  • 76
    • 0001613347 scopus 로고    scopus 로고
    • Pathogen-induced changes in the antioxidant status of the apoplast in barley leaves
    • Vanacker H., Carver T.L., and Foyer C.H. Pathogen-induced changes in the antioxidant status of the apoplast in barley leaves. Plant Physiology 117 (1998) 1103-1114
    • (1998) Plant Physiology , vol.117 , pp. 1103-1114
    • Vanacker, H.1    Carver, T.L.2    Foyer, C.H.3
  • 77
    • 0032998911 scopus 로고    scopus 로고
    • Changes in apoplastic antioxidants induced by powdery mildew attack in oat genotypes with race non-specific resistance
    • Vanacker H., Foyer C.H., and Carver T.L.M. Changes in apoplastic antioxidants induced by powdery mildew attack in oat genotypes with race non-specific resistance. Planta 208 (1998) 444-452
    • (1998) Planta , vol.208 , pp. 444-452
    • Vanacker, H.1    Foyer, C.H.2    Carver, T.L.M.3
  • 80
    • 12744268500 scopus 로고    scopus 로고
    • Differential targeting of GSH1 is achieved by multiple transcription initiation: Implications for the compartmentation of glutathione biosynthesis in the Brassicaceae
    • Wachter A., Wolf S., Steininger H., Bogs J., and Rausch T. Differential targeting of GSH1 is achieved by multiple transcription initiation: Implications for the compartmentation of glutathione biosynthesis in the Brassicaceae. The Plant Journal 41 (2005) 15-30
    • (2005) The Plant Journal , vol.41 , pp. 15-30
    • Wachter, A.1    Wolf, S.2    Steininger, H.3    Bogs, J.4    Rausch, T.5
  • 81
    • 0034624481 scopus 로고    scopus 로고
    • Vacuolar transport of the glutathione conjugate of trans-cinnamic acid
    • Walczak H.A., and Dean J.V. Vacuolar transport of the glutathione conjugate of trans-cinnamic acid. Phytochemistry 53 (2000) 441-446
    • (2000) Phytochemistry , vol.53 , pp. 441-446
    • Walczak, H.A.1    Dean, J.V.2
  • 82
    • 0030237918 scopus 로고    scopus 로고
    • Cloning of the cDNA and genomic clones for glutathione synthetase from Arabidopsis thaliana and complementation of a gsh2 mutant in fission yeast
    • Wang C.L., and Oliver D.J. Cloning of the cDNA and genomic clones for glutathione synthetase from Arabidopsis thaliana and complementation of a gsh2 mutant in fission yeast. Plant Molecular Biology 31 (1996) 1093-1104
    • (1996) Plant Molecular Biology , vol.31 , pp. 1093-1104
    • Wang, C.L.1    Oliver, D.J.2
  • 84
    • 0032170826 scopus 로고    scopus 로고
    • Glutathione metabolic genes coordinately respond to heavy metals and jasmonic acid in Arabidopsis
    • Xiang C., and Oliver D.J. Glutathione metabolic genes coordinately respond to heavy metals and jasmonic acid in Arabidopsis. The Plant Cell 10 (1998) 1539-1550
    • (1998) The Plant Cell , vol.10 , pp. 1539-1550
    • Xiang, C.1    Oliver, D.J.2
  • 85
    • 0034979751 scopus 로고    scopus 로고
    • The biological functions of glutathione revisited in Arabidopsis transgenic plants with altered glutathione levels
    • Xiang C., Werner B.L., Christensen E.M., and Oliver D.J. The biological functions of glutathione revisited in Arabidopsis transgenic plants with altered glutathione levels. Plant Physiology 126 (2001) 564-574
    • (2001) Plant Physiology , vol.126 , pp. 564-574
    • Xiang, C.1    Werner, B.L.2    Christensen, E.M.3    Oliver, D.J.4
  • 86
    • 55249112721 scopus 로고    scopus 로고
    • Subcellular immunocytochemical analysis detects the highest concentrations of glutathione in mitochondria and not in plastids
    • Zechmann B., Mauch F., Sticher L., and Muller M. Subcellular immunocytochemical analysis detects the highest concentrations of glutathione in mitochondria and not in plastids. Journal of Experimental Botany 59 (2008) 4017-4027
    • (2008) Journal of Experimental Botany , vol.59 , pp. 4017-4027
    • Zechmann, B.1    Mauch, F.2    Sticher, L.3    Muller, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.