메뉴 건너뛰기




Volumn 114, Issue 3, 1997, Pages 907-915

Biochemical characterization and subcellular localization of the red kidney bean purple acid phosphatase

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; ENZYME LOCALIZATION; ENZYME SUBSTRATE; GERMINATION; PHASEOLUS VULGARIS; PURPLE ACID PHOSPHATASE;

EID: 0031397435     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.114.3.907     Document Type: Article
Times cited : (66)

References (41)
  • 1
    • 0020020859 scopus 로고
    • Phosphorus-31 nuclear magnetic resonance of contractile systems
    • Barany M, Glonek T (1982) Phosphorus-31 nuclear magnetic resonance of contractile systems. Methods Enzymol 85: 647-649
    • (1982) Methods Enzymol , vol.85 , pp. 647-649
    • Barany, M.1    Glonek, T.2
  • 3
    • 0038409396 scopus 로고
    • Induction of acid phosphatase in cotton seedlings: Enzyme purification, subunit structure and kinetic properties
    • Bhargava R, Sachar RC (1987) Induction of acid phosphatase in cotton seedlings: enzyme purification, subunit structure and kinetic properties. Phytochemistry 26: 1293-1297
    • (1987) Phytochemistry , vol.26 , pp. 1293-1297
    • Bhargava, R.1    Sachar, R.C.2
  • 4
    • 0000941390 scopus 로고
    • Hydrolytic enzymes in plant disease resistance
    • T Kosuge, Nester EW, eds. Macmillan. New York
    • Boller T (1987) Hydrolytic enzymes in plant disease resistance. In T Kosuge, Nester EW, eds, Plant-Microbe Interactions. Macmillan. New York, pp 385-414
    • (1987) Plant-Microbe Interactions , pp. 385-414
    • Boller, T.1
  • 5
    • 0002102453 scopus 로고
    • Mineral nutrition of plants in soils and in culture media
    • FC Steward, ed. Academic Press, New York
    • Bould C, Hewitt EJ (1963) Mineral nutrition of plants in soils and in culture media, In FC Steward, ed, Plant Physiology - A Treatise, Vol 3. Academic Press, New York, pp 28-29
    • (1963) Plant Physiology - a Treatise , vol.3 , pp. 28-29
    • Bould, C.1    Hewitt, E.J.2
  • 7
    • 0029317065 scopus 로고
    • Unique structural features of red kidney bean purple acid phosphatase
    • Cashikar AG, Rao NM (1995) Unique structural features of red kidney bean purple acid phosphatase. Indian J Biochem Biophys 32: 130-136
    • (1995) Indian J Biochem Biophys , vol.32 , pp. 130-136
    • Cashikar, A.G.1    Rao, N.M.2
  • 8
    • 0030586786 scopus 로고    scopus 로고
    • Role of the inter-subunit disulphide bond in the unfolding pathway of dimeric red kidney bean purple acid phosphatase
    • Cashikar AG, Rao NM (1996a) Role of the inter-subunit disulphide bond in the unfolding pathway of dimeric red kidney bean purple acid phosphatase, Biochim Biophys Acta 1296: 76-84
    • (1996) Biochim Biophys Acta , vol.1296 , pp. 76-84
    • Cashikar, A.G.1    Rao, N.M.2
  • 9
    • 0029883558 scopus 로고    scopus 로고
    • Unfolding pathway in red kidney bean purple acid phosphatase is dependent on ligand binding
    • Cashikar AG, Rao NM (1996b) Unfolding pathway in red kidney bean purple acid phosphatase is dependent on ligand binding. J Biol Chem 271: 4741-4746
    • (1996) J Biol Chem , vol.271 , pp. 4741-4746
    • Cashikar, A.G.1    Rao, N.M.2
  • 10
    • 0009699231 scopus 로고
    • Simple enzyme kinetics
    • D Rickwood, ed. IRL Press, Oxford, UK
    • Cornish-Bowden A, Wharton CW (1988) Simple enzyme kinetics. In D Rickwood, ed, Enzyme Kinetics. IRL Press, Oxford, UK, pp 10-13
    • (1988) Enzyme Kinetics , pp. 10-13
    • Cornish-Bowden, A.1    Wharton, C.W.2
  • 12
    • 3543038980 scopus 로고
    • Identification of phosphate granules occurring in seedling tissue of two palm species (Phoenix dactylifera and Washingtonia filifera)
    • DeMason DA, Stillman JL (1986) Identification of phosphate granules occurring in seedling tissue of two palm species (Phoenix dactylifera and Washingtonia filifera). Planta 167: 321-329
    • (1986) Planta , vol.167 , pp. 321-329
    • Demason, D.A.1    Stillman, J.L.2
  • 13
    • 0026650480 scopus 로고
    • The soybean vegetative storage proteins VSPα and VSPβ are acid phosphatases active on polyphosphates
    • DeWald DB, Mason HS, Mullet JE (1992) The soybean vegetative storage proteins VSPα and VSPβ are acid phosphatases active on polyphosphates. J Biol Chem 267: 15958-15964
    • (1992) J Biol Chem , vol.267 , pp. 15958-15964
    • Dewald, D.B.1    Mason, H.S.2    Mullet, J.E.3
  • 14
    • 0000618327 scopus 로고
    • Purification and characterization of a phosphoenolpyruvate phosphatase from Brassica nigra suspension cells
    • Duff SMG, Lefebvre DD, Plaxton WC (1989) Purification and characterization of a phosphoenolpyruvate phosphatase from Brassica nigra suspension cells. Plant Physiol 90: 734-741
    • (1989) Plant Physiol , vol.90 , pp. 734-741
    • Duff, S.M.G.1    Lefebvre, D.D.2    Plaxton, W.C.3
  • 15
    • 0026004627 scopus 로고
    • Phosphate starvation response in plant cells: De novo synthesis and degradation of acid phosphatase
    • Duff SMG, Plaxton WC, Lefebvre DD (1991) Phosphate starvation response in plant cells: de novo synthesis and degradation of acid phosphatase. Proc Natl Acad Sci USA 88: 9538-9542
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9538-9542
    • Duff, S.M.G.1    Plaxton, W.C.2    Lefebvre, D.D.3
  • 16
    • 0027950058 scopus 로고
    • The role of acid phosphatases in plant phosphorus metabolism
    • Duff SMG, Sarath G, Plaxton WC (1994) The role of acid phosphatases in plant phosphorus metabolism. Physiol Plant 90: 791-800
    • (1994) Physiol Plant , vol.90 , pp. 791-800
    • Duff, S.M.G.1    Sarath, G.2    Plaxton, W.C.3
  • 18
    • 0028140651 scopus 로고
    • Purification and characterization of a potato tuber acid phosphatase having significant phosphotyrosine phosphatase activity
    • Gellatly K, Moorhead GBG, Duff SMG, Lefebvre DD, Plaxton WC (1994) Purification and characterization of a potato tuber acid phosphatase having significant phosphotyrosine phosphatase activity. Plant Physiol 106: 223-232
    • (1994) Plant Physiol , vol.106 , pp. 223-232
    • Gellatly, K.1    Moorhead, G.B.G.2    Duff, S.M.G.3    Lefebvre, D.D.4    Plaxton, W.C.5
  • 19
    • 0023957340 scopus 로고
    • Purification and characterization of phytase from cotyledons of germinating soybean seeds
    • Gibson DM, Ullah AHJ (1988) Purification and characterization of phytase from cotyledons of germinating soybean seeds. Arch Biochem Biophys 260: 503-513
    • (1988) Arch Biochem Biophys , vol.260 , pp. 503-513
    • Gibson, D.M.1    Ullah, A.H.J.2
  • 20
    • 51249172067 scopus 로고
    • Phosphate starvation stress as an experimental system for molecular analysis
    • Goldstein AH, Baertlein DA, Danon A (1989) Phosphate starvation stress as an experimental system for molecular analysis. Plant Mol Biol Rep 7: 7-16
    • (1989) Plant Mol Biol Rep , vol.7 , pp. 7-16
    • Goldstein, A.H.1    Baertlein, D.A.2    Danon, A.3
  • 21
    • 0038409395 scopus 로고
    • Multiple forms of acid phosphatase in cotyledons of Vigna mungo seedlings: Immunological detection and quantification
    • Haraguchi H, Yamauchi D, Minamikawa T (1990) Multiple forms of acid phosphatase in cotyledons of Vigna mungo seedlings: immunological detection and quantification. Plant Cell Physiol 31: 917-923
    • (1990) Plant Cell Physiol , vol.31 , pp. 917-923
    • Haraguchi, H.1    Yamauchi, D.2    Minamikawa, T.3
  • 22
    • 0013979409 scopus 로고
    • Inorganic polyphosphates in biology: Structure, metabolism and function
    • Harold FM (1966) Inorganic polyphosphates in biology: structure, metabolism and function. Bacteriol Rev 30: 772-794
    • (1966) Bacteriol Rev , vol.30 , pp. 772-794
    • Harold, F.M.1
  • 23
    • 0019830545 scopus 로고
    • A new and convenient colorimetric determination of inorganic orthophosphate and its application to the assay of inorganic pyrophosphatase
    • Heinonen JK, Lahiti RJ (1981) A new and convenient colorimetric determination of inorganic orthophosphate and its application to the assay of inorganic pyrophosphatase. Anal Biochem 113: 313-317
    • (1981) Anal Biochem , vol.113 , pp. 313-317
    • Heinonen, J.K.1    Lahiti, R.J.2
  • 25
    • 0027988448 scopus 로고
    • The amino acid sequence of the red kidney bean Fe(III)-Zn(II) purple acid phosphatase: Determination of the amino acid sequence by a combination off matrix-assisted laser desorption/ionization mass spectrometry and automated Edman sequencing
    • Klabunde T, Stahl B, Suerbaum H, Hahner S, Karas M, Hillemkamp F, Krebs B, Witzel H (1994) The amino acid sequence of the red kidney bean Fe(III)-Zn(II) purple acid phosphatase: determination of the amino acid sequence by a combination off matrix-assisted laser desorption/ionization mass spectrometry and automated Edman sequencing. Eur J Biochem 226: 369-375
    • (1994) Eur J Biochem , vol.226 , pp. 369-375
    • Klabunde, T.1    Stahl, B.2    Suerbaum, H.3    Hahner, S.4    Karas, M.5    Hillemkamp, F.6    Krebs, B.7    Witzel, H.8
  • 26
    • 0029003660 scopus 로고
    • Structural relationship between the mammalian Fe(III)-Fe(II) and the Fe(III)Zn(II) plant purple acid phosphatase
    • Klabunde T, Strater N, Krebs B, Witzel H (1995) Structural relationship between the mammalian Fe(III)-Fe(II) and the Fe(III)Zn(II) plant purple acid phosphatase. FEBS Lett 367: 56-60
    • (1995) FEBS Lett , vol.367 , pp. 56-60
    • Klabunde, T.1    Strater, N.2    Krebs, B.3    Witzel, H.4
  • 28
    • 0014901563 scopus 로고
    • Their phosphatase controversy: Love's labours lost
    • Novikoff AB (1970) Their phosphatase controversy: love's labours lost. J Histochem Cytochem 18: 916-917
    • (1970) J Histochem Cytochem , vol.18 , pp. 916-917
    • Novikoff, A.B.1
  • 29
    • 0002661197 scopus 로고
    • Purification and characterization of homogenous sunflower seed acid phosphatase
    • Park HC, van Etten RL (1986) Purification and characterization of homogenous sunflower seed acid phosphatase. Phytochemistry 25: 351-357
    • (1986) Phytochemistry , vol.25 , pp. 351-357
    • Park, H.C.1    Van Etten, R.L.2
  • 30
    • 3543005509 scopus 로고
    • Electron histochemistry (ultrahistochemistry)
    • Churchill Livingstone, Edinburgh, UK
    • Pearse AGE (1972) Electron histochemistry (ultrahistochemistry). In Histochemistry: Theoretical and Applied, Ed 3, Vol 2. Churchill Livingstone, Edinburgh, UK, pp 1280-1281
    • (1972) Histochemistry: Theoretical and Applied, Ed 3 , vol.2 , pp. 1280-1281
    • Pearse, A.G.E.1
  • 31
    • 0013816788 scopus 로고
    • Thermodynamic data for the secondary phosphate ionization of adenosine, guanosine, inosine, cytidine and uridine nucleotides and triphosphates
    • Phillips RSJ, Eisenberg P, George P, Rutman RJ (1965) Thermodynamic data for the secondary phosphate ionization of adenosine, guanosine, inosine, cytidine and uridine nucleotides and triphosphates. J Biol Chem 240: 4393-4397
    • (1965) J Biol Chem , vol.240 , pp. 4393-4397
    • Phillips, R.S.J.1    Eisenberg, P.2    George, P.3    Rutman, R.J.4
  • 32
    • 0026172013 scopus 로고
    • The (1→3) linked α-L-fucosyl group of the N-glycans of the Wistaria floribunda lectins recognized by a rabbit antiserum
    • Ramirez-Soto D, Poretz RD (1991) The (1→3) linked α-L-fucosyl group of the N-glycans of the Wistaria floribunda lectins recognized by a rabbit antiserum. Carbohydr Res 213: 27-36
    • (1991) Carbohydr Res , vol.213 , pp. 27-36
    • Ramirez-Soto, D.1    Poretz, R.D.2
  • 33
    • 0015218654 scopus 로고
    • 3-Phosphoglycerate phosphatase in plants. I. Isolation and characterization from sugar cane leaves
    • Randall DD, Tolbert NE (1971) 3-Phosphoglycerate phosphatase in plants. I. Isolation and characterization from sugar cane leaves. J Biol Chem 246: 5510-5517
    • (1971) J Biol Chem , vol.246 , pp. 5510-5517
    • Randall, D.D.1    Tolbert, N.E.2
  • 34
    • 0028206873 scopus 로고
    • The oligosaccharides of the Fe(III)-Zn(II) purple acid phosphatase of the red kidney bean: Determination of the structure by a combination of matrix-assisted laser desorption/ionization mass spectrometry and selective enzymic degradation
    • Stahl B, Klabunde T, Witzel H, Krebs B, Steup M, Karas M, Hillenkamp F (1994) The oligosaccharides of the Fe(III)-Zn(II) purple acid phosphatase of the red kidney bean: determination of the structure by a combination of matrix-assisted laser desorption/ionization mass spectrometry and selective enzymic degradation Eur J Biochem 220: 321-330
    • (1994) Eur J Biochem , vol.220 , pp. 321-330
    • Stahl, B.1    Klabunde, T.2    Witzel, H.3    Krebs, B.4    Steup, M.5    Karas, M.6    Hillenkamp, F.7
  • 35
    • 0029640070 scopus 로고
    • Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site
    • Strater N, Klabunde T, Tucker P, Witzel H, Krebs B (1995) Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site. Science 268: 1489-1492
    • (1995) Science , vol.268 , pp. 1489-1492
    • Strater, N.1    Klabunde, T.2    Tucker, P.3    Witzel, H.4    Krebs, B.5
  • 36
    • 0027336220 scopus 로고
    • Zn-exchange and Mossbauer studies on the [Fe-Fe] derivatives of the purple acid Fe(III)-Zn(II)-phosphatase from kidney beans
    • Suerbaum H, Korner M, Witzel H, Althaus E, Mosel B-D, Muller-Warmuth W (1993) Zn-exchange and Mossbauer studies on the [Fe-Fe] derivatives of the purple acid Fe(III)-Zn(II)-phosphatase from kidney beans. Eur J Biochem 214: 313-321
    • (1993) Eur J Biochem , vol.214 , pp. 313-321
    • Suerbaum, H.1    Korner, M.2    Witzel, H.3    Althaus, E.4    Mosel, B.-D.5    Muller-Warmuth, W.6
  • 37
    • 0023953770 scopus 로고
    • Purification and characterization of acid phosphatase from cotyledons of germinating soybean seeds
    • Ullah AH, Gibson DM (1988) Purification and characterization of acid phosphatase from cotyledons of germinating soybean seeds. Arch Biochem Biophys 260: 514-520
    • (1988) Arch Biochem Biophys , vol.260 , pp. 514-520
    • Ullah, A.H.1    Gibson, D.M.2
  • 38
    • 0025222988 scopus 로고
    • An enzyme with a double identity: Purple acid phosphatase and tartarate resistant acid phosphatase
    • Vincent JB, Averill BA (1990) An enzyme with a double identity: purple acid phosphatase and tartarate resistant acid phosphatase. FASEB J 4: 3009-3014
    • (1990) FASEB J , vol.4 , pp. 3009-3014
    • Vincent, J.B.1    Averill, B.A.2
  • 39
    • 0026535321 scopus 로고
    • Hydrolysis of phosphate monoesters: A biological problem with multiple chemical solutions
    • Vincent JB, Crowder MW, Averill BA (1992) Hydrolysis of phosphate monoesters: a biological problem with multiple chemical solutions. Trends Biochem Sci 17: 105-110
    • (1992) Trends Biochem Sci , vol.17 , pp. 105-110
    • Vincent, J.B.1    Crowder, M.W.2    Averill, B.A.3
  • 40
    • 0023937323 scopus 로고
    • Biological aspects of inorganic polyphosphates
    • Wood HG, Clark JE (1988) Biological aspects of inorganic polyphosphates. Annu Rev Biochem 57: 235-260
    • (1988) Annu Rev Biochem , vol.57 , pp. 235-260
    • Wood, H.G.1    Clark, J.E.2
  • 41
    • 0024344057 scopus 로고
    • A novel acid phosphatase excreted by Penicillium funiculosum that hydrolyzes both phosphodiesters and phosphomonoesters with aryl leaving groups
    • Yoshida H, Oikawa S, Ikeda M, Reese ET (1989) A novel acid phosphatase excreted by Penicillium funiculosum that hydrolyzes both phosphodiesters and phosphomonoesters with aryl leaving groups. J Biochem 105: 794-798
    • (1989) J Biochem , vol.105 , pp. 794-798
    • Yoshida, H.1    Oikawa, S.2    Ikeda, M.3    Reese, E.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.