메뉴 건너뛰기




Volumn 67, Issue 1, 2000, Pages 13-24

Inhibition of enzymes of the glycolytic pathway and hexose monophosphate bypass by phosphonate

Author keywords

Enzyme linked assays; Glycolysis; Phosphogluconate pathway; Phosphonate; Phytophthora palmivora

Indexed keywords


EID: 0034046093     PISSN: 00483575     EISSN: None     Source Type: Journal    
DOI: 10.1006/pest.1999.2465     Document Type: Article
Times cited : (24)

References (29)
  • 1
    • 0013611039 scopus 로고
    • In vitro antifungal activity of fosetyl Al and phosphorus acid in Phytophthora spp
    • Bompeix G., Saindrenan P. In vitro antifungal activity of fosetyl Al and phosphorus acid in Phytophthora spp. Fruits. 39:1984;777.
    • (1984) Fruits , vol.39 , pp. 777
    • Bompeix, G.1    Saindrenan, P.2
  • 2
    • 0000464222 scopus 로고
    • Studies on the in vitro and in vivo antifungal activity of fosetyl Al and phosphorous acid
    • Fenn M. E., Coffey M. D. Studies on the in vitro and in vivo antifungal activity of fosetyl Al and phosphorous acid. Phytopatholgy. 74:1984;606.
    • (1984) Phytopatholgy , vol.74 , pp. 606
    • Fenn, M.E.1    Coffey, M.D.2
  • 3
    • 0028065652 scopus 로고
    • Sensitivity of Fusarium oxysporum f. sp. cubense to phosphonate
    • Davis A. J., Say M., Snow A. J., Grant B. R. Sensitivity of Fusarium oxysporum f. sp. cubense to phosphonate. Plant Pathol. 43:1994;200.
    • (1994) Plant Pathol. , vol.43 , pp. 200
    • Davis, A.J.1    Say, M.2    Snow, A.J.3    Grant, B.R.4
  • 4
    • 0001630217 scopus 로고
    • Systemic fungicides and the control of oomycetes
    • Cohen Y., Coffey M. D. Systemic fungicides and the control of oomycetes. Annu. Rev. Phytopathol. 24:1986;311.
    • (1986) Annu. Rev. Phytopathol. , vol.24 , pp. 311
    • Cohen, Y.1    Coffey, M.D.2
  • 6
    • 0025289852 scopus 로고
    • Alterations in nucleotide and pyrophosphate levels in Phytophthora palmivora following exposure to the antifungal agent potassium phosphonate (phosphite)
    • Griffith J. M., Smillie R. H., Grant B. R. Alterations in nucleotide and pyrophosphate levels in Phytophthora palmivora following exposure to the antifungal agent potassium phosphonate (phosphite). J. Gen. Microbiol. 136:1990;1285.
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 1285
    • Griffith, J.M.1    Smillie, R.H.2    Grant, B.R.3
  • 8
    • 0000107757 scopus 로고
    • Physiological responses of Phytophthora citrophthora to subinhibitory concentrations of phosphonate
    • Barchietto T., Saindrenan P., Bompeix G. Physiological responses of Phytophthora citrophthora to subinhibitory concentrations of phosphonate. Pestic. Biochem. Physiol. 42:1992;151.
    • (1992) Pestic. Biochem. Physiol. , vol.42 , pp. 151
    • Barchietto, T.1    Saindrenan, P.2    Bompeix, G.3
  • 9
    • 0027963239 scopus 로고
    • The effect of phosphonate on the acid soluble phosphorous components in the genus Phytophthora
    • Niere J. O., De Angelis G., Grant B. R. The effect of phosphonate on the acid soluble phosphorous components in the genus Phytophthora. Microbiology. 140:1994;1661.
    • (1994) Microbiology , vol.140 , pp. 1661
    • Niere, J.O.1    De Angelis, G.2    Grant, B.R.3
  • 10
    • 0342988235 scopus 로고
    • Rapid appearance of novel sugars on exposure of the pseudo fungus Phytophthora palmivora to phosphonate
    • Griffith J. M., De Angelis G., Niere J. O., Grant B. R. Rapid appearance of novel sugars on exposure of the pseudo fungus Phytophthora palmivora to phosphonate. Aust. Microbiol. 15:1994;142.
    • (1994) Aust. Microbiol. , vol.15 , pp. 142
    • Griffith, J.M.1    De Angelis, G.2    Niere, J.O.3    Grant, B.R.4
  • 11
    • 0032169386 scopus 로고    scopus 로고
    • Inhibition of inorganic pyrophosphate by phosphonate - A site of action in Phytophthora spp.?
    • Martin H., Grant B. R., Stehmann C. Inhibition of inorganic pyrophosphate by phosphonate - A site of action in Phytophthora spp.? Pesticide Biochem. Physiol. 61:1998;65.
    • (1998) Pesticide Biochem. Physiol. , vol.61 , pp. 65
    • Martin, H.1    Grant, B.R.2    Stehmann, C.3
  • 12
    • 0027207008 scopus 로고
    • Phosphonate inhibitors of glyceraldehyde 3-phosphate dehydrogenase and phosphoglycerate kinase
    • Li Y. K., Byers L. D. Phosphonate inhibitors of glyceraldehyde 3-phosphate dehydrogenase and phosphoglycerate kinase. Biochim. Biophys. Acta. 1164:1993;17.
    • (1993) Biochim. Biophys. Acta , vol.1164 , pp. 17
    • Li, Y.K.1    Byers, L.D.2
  • 13
    • 0001422064 scopus 로고
    • Glucose 6-phosphate dehydrogenase
    • J. Bergmeyer, Grassl M. Weinheim: Verlag Chemie
    • Deutsch J. Glucose 6-phosphate dehydrogenase. Bergmeyer J., Grassl M. Methods of Enzymatic Analysis. IV:1983;190-197 Verlag Chemie, Weinheim.
    • (1983) Methods of Enzymatic Analysis , vol.4 , pp. 190-197
    • Deutsch, J.1
  • 14
    • 0000212377 scopus 로고    scopus 로고
    • Appearance of novel glucose 6-phosphate dehydrogenase isoforms in Chlamydomonas reinhardtii during growth on nitrate
    • Huppe H. C., Turpin D. H. Appearance of novel glucose 6-phosphate dehydrogenase isoforms in Chlamydomonas reinhardtii during growth on nitrate. Plant Physiol. 110:1996;1431.
    • (1996) Plant Physiol. , vol.110 , pp. 1431
    • Huppe, H.C.1    Turpin, D.H.2
  • 15
    • 17544363922 scopus 로고    scopus 로고
    • Alterations of enzyme function of the type II hexokinase C-terminal half on replacements of restricted regions by corresponding regions of glucokinase
    • Kogure K., Yamamoto K., Majima E., Shinohara Y., Yamashita K., Terada H. Alterations of enzyme function of the type II hexokinase C-terminal half on replacements of restricted regions by corresponding regions of glucokinase. J. Biol. Chem. 271:1996;15230.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15230
    • Kogure, K.1    Yamamoto, K.2    Majima, E.3    Shinohara, Y.4    Yamashita, K.5    Terada, H.6
  • 16
    • 0006816375 scopus 로고
    • 6-phosphogluconate dehydrogenase
    • Bergmeyer H. U. Weinheim: Verlag Chemie
    • King J. 6-phosphogluconate dehydrogenase. Bergmeyer H. U. Methods of Enzymatic Analysis. II:1974;632-635 Verlag Chemie, Weinheim.
    • (1974) Methods of Enzymatic Analysis , vol.2 , pp. 632-635
    • King, J.1
  • 17
    • 0028038878 scopus 로고
    • Purification and characterization of phosphoglucomutase from peas
    • Galloway C. M., Dugger W. M. Purification and characterization of phosphoglucomutase from peas. Physiol. Plant. 92:1994;479.
    • (1994) Physiol. Plant. , vol.92 , pp. 479
    • Galloway, C.M.1    Dugger, W.M.2
  • 18
    • 0030250591 scopus 로고    scopus 로고
    • Purification and characterization of pyrophosphate dependent phosphofructokinase from phosphate-starved Brassica nigra suspension cells
    • Theodorou M. E., Plaxton W. C. Purification and characterization of pyrophosphate dependent phosphofructokinase from phosphate-starved Brassica nigra suspension cells. Plant Physiol. 112:1996;343.
    • (1996) Plant Physiol. , vol.112 , pp. 343
    • Theodorou, M.E.1    Plaxton, W.C.2
  • 19
    • 0029257325 scopus 로고
    • Errors and artifacts in coupled spectrophotometric assays and enzyme activity
    • Kruger N. J. Errors and artifacts in coupled spectrophotometric assays and enzyme activity. Phytochemistry. 38:1994;1065.
    • (1994) Phytochemistry , vol.38 , pp. 1065
    • Kruger, N.J.1
  • 20
    • 0029990572 scopus 로고    scopus 로고
    • The mechanism of velocity modulated allosteric regulation in D-3-phosphoglycerate dehydrogenase
    • Al-Rabiee R., Lee E. J., Grant G. A. The mechanism of velocity modulated allosteric regulation in D-3-phosphoglycerate dehydrogenase. J. Biol. Chem. 271:1996;13013.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13013
    • Al-Rabiee, R.1    Lee, E.J.2    Grant, G.A.3
  • 21
    • 0004176971 scopus 로고
    • New York: Harper & Row. p. 578
    • Rawn J. D. Biochemistry. 1983;Harper & Row, New York. p. 578.
    • (1983) Biochemistry
    • Rawn, J.D.1
  • 22
    • 0002677837 scopus 로고
    • On the metabolic significance of phosphorolytic and pyrophosphorolytic reactions
    • H. Kasha, Pullman B. New York: Academic Press
    • Kornberg A. On the metabolic significance of phosphorolytic and pyrophosphorolytic reactions. Kasha H., Pullman B. Horizons in Biochemistry. 1962;251-264 Academic Press, New York.
    • (1962) Horizons in Biochemistry , pp. 251-264
    • Kornberg, A.1
  • 23
    • 0027198160 scopus 로고
    • Pyrophosphate-dependent phosphofructokinase from the amoeba Naegleria fowleri, an AMP-sensitive enzyme
    • Mertens E., De Jonckheere J., Van Schaftingen E. Pyrophosphate-dependent phosphofructokinase from the amoeba Naegleria fowleri, an AMP-sensitive enzyme. Biochem. J. 292:1993;797.
    • (1993) Biochem. J. , vol.292 , pp. 797
    • Mertens, E.1    De Jonckheere, J.2    Van Schaftingen, E.3
  • 25
    • 85052243133 scopus 로고
    • Target sites of fungicides to control oomycetes
    • Köller W. Boca Raton: CRC Press
    • Griffith J. M., Davis A. J., Grant B. R. Target sites of fungicides to control oomycetes. Köller W. Target Sites of Fungicide Action. 1992;69-100 CRC Press, Boca Raton.
    • (1992) Target Sites of Fungicide Action , pp. 69-100
    • Griffith, J.M.1    Davis, A.J.2    Grant, B.R.3
  • 26
    • 0029999407 scopus 로고    scopus 로고
    • Enzymic and molecular characterization of NADP-dependent glyceraldehyde 3-phosphate dehydrogenase from Synechococcus PCC 7942: Resistance of the enzyme to hydrogen peroxide
    • Tamoi M., Ishikawa T., Takeda T., Shigeoka S. Enzymic and molecular characterization of NADP-dependent glyceraldehyde 3-phosphate dehydrogenase from Synechococcus PCC 7942: Resistance of the enzyme to hydrogen peroxide. Biochem. J. 316:1996;685.
    • (1996) Biochem. J. , vol.316 , pp. 685
    • Tamoi, M.1    Ishikawa, T.2    Takeda, T.3    Shigeoka, S.4
  • 27
    • 0029951973 scopus 로고    scopus 로고
    • Pyrophosphate-dependent phosphofructokinase of Entamoeba histolytica: Molecular cloning, recombinant expression and inhibition by pyrophosphate analogues
    • Bruchhaus I., Jacobs T., Denart M., Tannich E. Pyrophosphate-dependent phosphofructokinase of Entamoeba histolytica: Molecular cloning, recombinant expression and inhibition by pyrophosphate analogues. Biochem. J. 316:1996;57.
    • (1996) Biochem. J. , vol.316 , pp. 57
    • Bruchhaus, I.1    Jacobs, T.2    Denart, M.3    Tannich, E.4
  • 28
    • 0001045529 scopus 로고
    • Product inhibition of potato tuber pyrophosphate: Fructose-6-phosphate phosphotransferase by phosphate and pyrophosphate
    • Stitt M. Product inhibition of potato tuber pyrophosphate: Fructose-6-phosphate phosphotransferase by phosphate and pyrophosphate. Plant Physiol. 89:1989;628.
    • (1989) Plant Physiol. , vol.89 , pp. 628
    • Stitt, M.1
  • 29
    • 0027363590 scopus 로고
    • Phosphonate inhibition as a function of phosphate concentration in isolates of Phytophthora palmivora
    • Griffith J. M., Coffey M. D., Grant B. R. Phosphonate inhibition as a function of phosphate concentration in isolates of Phytophthora palmivora. J. Gen Microbiol. 139:1993;2106.
    • (1993) J. Gen Microbiol. , vol.139 , pp. 2106
    • Griffith, J.M.1    Coffey, M.D.2    Grant, B.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.