메뉴 건너뛰기




Volumn 114, Issue 4, 1997, Pages 1237-1245

Purification and characterization of a novel class III peroxidase isoenzyme from tea leaves

Author keywords

[No Author keywords available]

Indexed keywords

ASCORBIC ACID; CHARACTERIZATION; HOMOGENEITY; ISOENZYME; OXIDATION; PEROXIDASE; PLANT LEAF; PURIFICATION; SECONDARY METABOLITE; TEA;

EID: 0031200793     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.114.4.1237     Document Type: Article
Times cited : (117)

References (40)
  • 1
    • 0028055996 scopus 로고
    • Separate assays specific for ascorbate peroxidase and guaiacol peroxidase and for the chloroplastic and cytosolic isozymes of ascorbate peroxidase in plants
    • Amako K, Chen G, Asada K (1994) Separate assays specific for ascorbate peroxidase and guaiacol peroxidase and for the chloroplastic and cytosolic isozymes of ascorbate peroxidase in plants. Plant Cell Physiol 35: 497-504
    • (1994) Plant Cell Physiol , vol.35 , pp. 497-504
    • Amako, K.1    Chen, G.2    Asada, K.3
  • 2
    • 0024296184 scopus 로고
    • Studies on compound I formation of the lignin peroxidase from Phanerochaete chrysosporium
    • Andrawis A, Johnson KA, Tien M (1988) Studies on compound I formation of the lignin peroxidase from Phanerochaete chrysosporium. J Biol Chem 263: 1195-1198
    • (1988) J Biol Chem , vol.263 , pp. 1195-1198
    • Andrawis, A.1    Johnson, K.A.2    Tien, M.3
  • 3
    • 84983392009 scopus 로고
    • Ascorbate peroxidase-a hydrogen peroxidescavenging enzyme in plants
    • Asada K (1992) Ascorbate peroxidase-a hydrogen peroxidescavenging enzyme in plants. Physiol Plant 85: 235-241
    • (1992) Physiol Plant , vol.85 , pp. 235-241
    • Asada, K.1
  • 5
    • 0030087896 scopus 로고    scopus 로고
    • Ascorbate peroxidase. A prominent membrane protein in oilseed glyoxysomes
    • Bunkelmann JR, Trelease RN (1996) Ascorbate peroxidase. A prominent membrane protein in oilseed glyoxysomes. Plant Physiol 110: 589-598
    • (1996) Plant Physiol , vol.110 , pp. 589-598
    • Bunkelmann, J.R.1    Trelease, R.N.2
  • 6
    • 0025317811 scopus 로고
    • Hydroxyurea and p-aminophenol are the suicide inhibitors of ascorbate peroxidase
    • Chen G, Asada K (1990) Hydroxyurea and p-aminophenol are the suicide inhibitors of ascorbate peroxidase. J Biol Chem 265: 2775-2781
    • (1990) J Biol Chem , vol.265 , pp. 2775-2781
    • Chen, G.1    Asada, K.2
  • 7
    • 33745314723 scopus 로고
    • Ascorbate peroxidase in tea leaves: Occurrence of two isozymes and the differences in their enzymatic and molecular properties
    • Chen GX, Asada K (1989) Ascorbate peroxidase in tea leaves: occurrence of two isozymes and the differences in their enzymatic and molecular properties. Plant Cell Physiol 30: 987-998
    • (1989) Plant Cell Physiol , vol.30 , pp. 987-998
    • Chen, G.X.1    Asada, K.2
  • 8
    • 0013505129 scopus 로고
    • The amino acid sequence of ascorbate peroxidase from tea has a high degree of homology to that of cytochrome c peroxidase from yeast
    • Chen GX, Satoshi S, Asada K (1992) The amino acid sequence of ascorbate peroxidase from tea has a high degree of homology to that of cytochrome c peroxidase from yeast. Plant Cell Physiol 32: 109-116
    • (1992) Plant Cell Physiol , vol.32 , pp. 109-116
    • Chen, G.X.1    Satoshi, S.2    Asada, K.3
  • 9
    • 0000996814 scopus 로고
    • Studies on horseradish peroxidase, XI. on the nature of compounds I and II as determined from the kinetics of the oxidation of ferrocyanide
    • Cotton ML, Dunford HB (1973) Studies on horseradish peroxidase, XI. On the nature of compounds I and II as determined from the kinetics of the oxidation of ferrocyanide. Can J Chem 51:582-587
    • (1973) Can J Chem , vol.51 , pp. 582-587
    • Cotton, M.L.1    Dunford, H.B.2
  • 10
    • 0000019955 scopus 로고
    • Purification, properties and distribution of ascorbate peroxidase in legume root nodules
    • Dalton DA, Hanus FJ, Russell SA, Evans H (1987) Purification, properties and distribution of ascorbate peroxidase in legume root nodules. Plant Physiol 83: 789-794
    • (1987) Plant Physiol , vol.83 , pp. 789-794
    • Dalton, D.A.1    Hanus, F.J.2    Russell, S.A.3    Evans, H.4
  • 11
    • 0002668438 scopus 로고
    • Soluble ascorbate peroxidase from potato tubers
    • Elia MR, Borraccino G, Dipierro S (1992) Soluble ascorbate peroxidase from potato tubers. Plant Sci 85: 17-21
    • (1992) Plant Sci , vol.85 , pp. 17-21
    • Elia, M.R.1    Borraccino, G.2    Dipierro, S.3
  • 12
    • 0002423269 scopus 로고    scopus 로고
    • Is ascorbate peroxidase only a scavenger of hydrogen peroxide?
    • C Obinger, U Burner, R Ebermann, C Penel, H Greppin, eds, University of Agriculture, Vienna, and University of Geneva, Switzerland
    • Gara L, Pinto MC, Paciolla C, Cappetti V, Arrigoni O (1996) Is ascorbate peroxidase only a scavenger of hydrogen peroxide? In C Obinger, U Burner, R Ebermann, C Penel, H Greppin, eds, Plant Peroxidases: Biochemistry and Physiology, Fourth International Symposium Proceedings. University of Agriculture, Vienna, and University of Geneva, Switzerland, pp 157-162
    • (1996) Plant Peroxidases: Biochemistry and Physiology, Fourth International Symposium Proceedings , pp. 157-162
    • Gara, L.1    Pinto, M.C.2    Paciolla, C.3    Cappetti, V.4    Arrigoni, O.5
  • 13
    • 0030111427 scopus 로고    scopus 로고
    • Purification and unusual kinetic properties of a tobacco anionic peroxidase
    • Gazaryan IG, Lagrimini LM (1996) Purification and unusual kinetic properties of a tobacco anionic peroxidase. Phytochemistry 41: 1029-1034
    • (1996) Phytochemistry , vol.41 , pp. 1029-1034
    • Gazaryan, I.G.1    Lagrimini, L.M.2
  • 14
    • 0030031097 scopus 로고    scopus 로고
    • The mechanism of indole-3-acetic acid oxidation by plant peroxidases. Anaerobic stopped-flow spectrophotometric studies on horseradish and tobacco peroxidases
    • Gazaryan IG, Lagrimini LM, Ashby GA, Thorneley RNF (1996) The mechanism of indole-3-acetic acid oxidation by plant peroxidases. Anaerobic stopped-flow spectrophotometric studies on horseradish and tobacco peroxidases. Biochem J 313: 841-847
    • (1996) Biochem J , vol.313 , pp. 841-847
    • Gazaryan, I.G.1    Lagrimini, L.M.2    Ashby, G.A.3    Thorneley, R.N.F.4
  • 16
    • 0026844641 scopus 로고
    • CDNA, amino acid and carbohydrate sequence of barley seedspecific peroxidase BP 1
    • Johansson A, Rasmussen SK, Harthill JE, Welinder KG (1992) cDNA, amino acid and carbohydrate sequence of barley seedspecific peroxidase BP 1. Plant Mol Biol 18: 1151-1161
    • (1992) Plant Mol Biol , vol.18 , pp. 1151-1161
    • Johansson, A.1    Rasmussen, S.K.2    Harthill, J.E.3    Welinder, K.G.4
  • 17
    • 0008835820 scopus 로고    scopus 로고
    • Bioactive potentiality of POD products derived from natural simple phenolics
    • C Obinger, U Burner, R Ebermann, C Penel, H Greppin, eds, University of Agriculture, Vienna, and University of Geneva, Switzerland
    • Kobayashi A, Fukusaki E, Kajiyama S (1996) Bioactive potentiality of POD products derived from natural simple phenolics. In C Obinger, U Burner, R Ebermann, C Penel, H Greppin, eds, Plant Peroxidases: Biochemistry and Physiology, Fourth International Symposium Proceedings. University of Agriculture, Vienna, and University of Geneva, Switzerland, pp 292-297
    • (1996) Plant Peroxidases: Biochemistry and Physiology, Fourth International Symposium Proceedings , pp. 292-297
    • Kobayashi, A.1    Fukusaki, E.2    Kajiyama, S.3
  • 18
    • 0001015272 scopus 로고
    • Cytosolic ascorbate peroxidase in seedlings and leaves of maize (Zea mays)
    • Koshiba T (1993) Cytosolic ascorbate peroxidase in seedlings and leaves of maize (Zea mays). Plant Cell Physiol 34: 713-721
    • (1993) Plant Cell Physiol , vol.34 , pp. 713-721
    • Koshiba, T.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0000155139 scopus 로고
    • Molecular cloning of complementary DNA encoding the ligninforming peroxidase from tobacco: Molecular analysis and tissue specific expression
    • Lagrimini LM, Burkhart W, Moyer M, Rothstein S (1987) Molecular cloning of complementary DNA encoding the ligninforming peroxidase from tobacco: molecular analysis and tissue specific expression. Proc Natl Acad Sci USA 84: 7542-7546
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7542-7546
    • Lagrimini, L.M.1    Burkhart, W.2    Moyer, M.3    Rothstein, S.4
  • 21
    • 0030200341 scopus 로고    scopus 로고
    • Kinetic and spectral properties of pea cytosolic ascorbate peroxidase
    • Marquez LA, Quitoriano M, Zilinskas BA, Dunford HB (1996) Kinetic and spectral properties of pea cytosolic ascorbate peroxidase. FEBS Lett 389: 153-156
    • (1996) FEBS Lett , vol.389 , pp. 153-156
    • Marquez, L.A.1    Quitoriano, M.2    Zilinskas, B.A.3    Dunford, H.B.4
  • 22
    • 0030043478 scopus 로고    scopus 로고
    • Ascorbate is the natural substrate for plant peroxidases
    • Mehlhorn H, Lelandais M, Korth HG, Foyer CH (1996) Ascorbate is the natural substrate for plant peroxidases. FEBS Lett 378: 203-206
    • (1996) FEBS Lett , vol.378 , pp. 203-206
    • Mehlhorn, H.1    Lelandais, M.2    Korth, H.G.3    Foyer, C.H.4
  • 23
    • 0025824122 scopus 로고
    • Molecular cloning and nucleotide sequence analysis of a cDNA encoding pea cytosolic ascorbate peroxidase
    • Mittler R, Zilinskas BA (1991a) Molecular cloning and nucleotide sequence analysis of a cDNA encoding pea cytosolic ascorbate peroxidase. FEBS Lett 289: 257-259
    • (1991) FEBS Lett , vol.289 , pp. 257-259
    • Mittler, R.1    Zilinskas, B.A.2
  • 24
    • 0000121196 scopus 로고
    • Purification and characterization of pea cytosolic ascorbate peroxidase
    • Mittler R, Zilinskas BA (1991b) Purification and characterization of pea cytosolic ascorbate peroxidase. Plant Physiol 97: 962-968
    • (1991) Plant Physiol , vol.97 , pp. 962-968
    • Mittler, R.1    Zilinskas, B.A.2
  • 25
    • 0029822638 scopus 로고    scopus 로고
    • Inactivation mechanism of ascorbate peroxidase at low concentrations of ascorbate: Hydrogen peroxide decomposes compound I of ascorbate peroxidase
    • Miyake C, Asada K (1996) Inactivation mechanism of ascorbate peroxidase at low concentrations of ascorbate: hydrogen peroxide decomposes compound I of ascorbate peroxidase. Plant Cell Physiol 37: 423-430
    • (1996) Plant Cell Physiol , vol.37 , pp. 423-430
    • Miyake, C.1    Asada, K.2
  • 26
    • 0001073890 scopus 로고
    • Purification and molecular properties of the thylakoid-bound ascorbate peroxidase in spinach chloroplasts
    • Miyake C, Cao W, Asada K (1993) Purification and molecular properties of the thylakoid-bound ascorbate peroxidase in spinach chloroplasts. Plant Cell Physiol 34: 881-889
    • (1993) Plant Cell Physiol , vol.34 , pp. 881-889
    • Miyake, C.1    Cao, W.2    Asada, K.3
  • 27
    • 3042993376 scopus 로고    scopus 로고
    • The homologous tryptophan critical for cytochrome c peroxidase function is not essential for ascorbate peroxidase activity
    • Pappa H, Patterson WR, Poulos TL (1996) The homologous tryptophan critical for cytochrome c peroxidase function is not essential for ascorbate peroxidase activity. J Bioinorg Chem 1: 61-66
    • (1996) J Bioinorg Chem , vol.1 , pp. 61-66
    • Pappa, H.1    Patterson, W.R.2    Poulos, T.L.3
  • 28
    • 0028901185 scopus 로고
    • Crystal structure of recombinant pea cytosolic ascorbate peroxidase
    • Patterson WR, Poulos TL (1995) Crystal structure of recombinant pea cytosolic ascorbate peroxidase. Biochemistry 34: 4331-4341
    • (1995) Biochemistry , vol.34 , pp. 4331-4341
    • Patterson, W.R.1    Poulos, T.L.2
  • 29
    • 0028913020 scopus 로고
    • Identification of a porphyrin Π cation radical in ascorbate peroxidase compound I
    • Patterson WR, Poulos TL, Goodin DB (1995) Identification of a porphyrin Π cation radical in ascorbate peroxidase compound I. Biochemistry 34: 4342-4345
    • (1995) Biochemistry , vol.34 , pp. 4342-4345
    • Patterson, W.R.1    Poulos, T.L.2    Goodin, D.B.3
  • 30
    • 0000756628 scopus 로고
    • The molar light absorption of pyridine ferroprotoporphyrin (pyridine haemochromogen)
    • Paul KG, Theorell H, Akeson A (1953) The molar light absorption of pyridine ferroprotoporphyrin (pyridine haemochromogen). Acta Chem Scand 7: 1284-1287
    • (1953) Acta Chem Scand , vol.7 , pp. 1284-1287
    • Paul, K.G.1    Theorell, H.2    Akeson, A.3
  • 31
    • 0027514159 scopus 로고
    • Crystallographic refinement of lignin peroxidase at 2 Å
    • Poulos TL, Edwards SL, Wariishi H, Gold MH (1993) Crystallographic refinement of lignin peroxidase at 2 Å. J Biol Chem 268: 4429-4440
    • (1993) J Biol Chem , vol.268 , pp. 4429-4440
    • Poulos, T.L.1    Edwards, S.L.2    Wariishi, H.3    Gold, M.H.4
  • 32
    • 85038529491 scopus 로고
    • Natural inhibitors of polyphenol oxidase and peroxidase activities
    • I Gassieva, G Kvesitadze, eds, Metsniereba, Tbilisi, Georgia
    • Pruidze GN (1987) Natural inhibitors of polyphenol oxidase and peroxidase activities. In I Gassieva, G Kvesitadze, eds, Tea Redox Enzymes. Metsniereba, Tbilisi, Georgia, pp 85-100
    • (1987) Tea Redox Enzymes , pp. 85-100
    • Pruidze, G.N.1
  • 33
    • 0022522916 scopus 로고
    • Spectral characterization of the oxidized states of lignin peroxidase, an extracellular heme enzyme from the white rot basidiomycete Phanerochaete chrysosporium
    • Renganathan V, Gold M (1986) Spectral characterization of the oxidized states of lignin peroxidase, an extracellular heme enzyme from the white rot basidiomycete Phanerochaete chrysosporium. Biochemistry 25: 1626-1631
    • (1986) Biochemistry , vol.25 , pp. 1626-1631
    • Renganathan, V.1    Gold, M.2
  • 37
    • 49749199032 scopus 로고
    • Cleavage of the haem-protein link by acid methylethylketone
    • Teale FWJ (1959) Cleavage of the haem-protein link by acid methylethylketone. Biochem Biophys 35: 543
    • (1959) Biochem Biophys , vol.35 , pp. 543
    • Teale, F.W.J.1
  • 38
    • 0025343321 scopus 로고
    • Lignin peroxidase H2 from Phanerochaete chrysosporium: Purification, characterization and stability to temperature and pH
    • Tuisel H, Sinclair R, Bumpus JA, Ashbaugh W, Brock BJ, Aust SD (1990) Lignin peroxidase H2 from Phanerochaete chrysosporium: purification, characterization and stability to temperature and pH. Arch Biochem Biophys 279: 158-166
    • (1990) Arch Biochem Biophys , vol.279 , pp. 158-166
    • Tuisel, H.1    Sinclair, R.2    Bumpus, J.A.3    Ashbaugh, W.4    Brock, B.J.5    Aust, S.D.6
  • 39
    • 0018488111 scopus 로고
    • Amino acid sequence studies of horseradish peroxidase
    • Welinder KG (1979) Amino acid sequence studies of horseradish peroxidase. Eur J Biochem 96: 483-502
    • (1979) Eur J Biochem , vol.96 , pp. 483-502
    • Welinder, K.G.1
  • 40
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases
    • Welinder KG (1992) Superfamily of plant, fungal and bacterial peroxidases. Curr Opin Struct Biol 2: 388-393
    • (1992) Curr Opin Struct Biol , vol.2 , pp. 388-393
    • Welinder, K.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.