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Volumn 1656, Issue 2-3, 2004, Pages 156-165

Inhibition studies on Rhodospirillum rubrum H+-pyrophosphatase expressed in Escherichia coli

Author keywords

H+ PPase; Inhibition; inorganic pyrophosphatase; inorganic pyrophosphate; PPase; PPi; proton pumping inorganic pyrophosphatase; Proton pumping pyrophosphatase; Rhodospirillum rubrum; Site specific mutant; Substrate preference

Indexed keywords

4 BROMOPHENACYL BROMIDE; BACTERIAL ENZYME; DICYCLOHEXYLCARBODIIMIDE; DIETHYL PYROCARBONATE; ENZYME VARIANT; FLUORESCEIN ISOTHIOCYANATE; HISTIDINE; INORGANIC PYROPHOSPHATASE; MAGNESIUM DERIVATIVE;

EID: 2642513841     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2004.03.005     Document Type: Article
Times cited : (7)

References (46)
  • 3
    • 0035209342 scopus 로고    scopus 로고
    • +-pyrophosphatases: From the evolutionary backwaters into the mainstream
    • +-pyrophosphatases: from the evolutionary backwaters into the mainstream. Trends Plant Sci. 6:2001;206-211
    • (2001) Trends Plant Sci. , vol.6 , pp. 206-211
    • Drozdowicz, Y.M.1    Rea, P.A.2
  • 4
    • 0015509099 scopus 로고
    • Proton-translocating pyrophosphatase from Rhodospirillum rubrum
    • Moyle J., Mitchell R., Mitchell P. Proton-translocating pyrophosphatase from Rhodospirillum rubrum. FEBS Lett. 1972;233-236
    • (1972) FEBS Lett. , pp. 233-236
    • Moyle, J.1    Mitchell, R.2    Mitchell, P.3
  • 8
    • 0013978142 scopus 로고
    • Light-induced energy conversion and the inorganic pyrophosphatase reaction in chromatophores from Rhodospirillum rubrum
    • Baltscheffsky M., Baltscheffsky H., von Stedingk L.-V. Light-induced energy conversion and the inorganic pyrophosphatase reaction in chromatophores from Rhodospirillum rubrum. Brookhaven Symp. 19:1966;246-257
    • (1966) Brookhaven Symp. , vol.19 , pp. 246-257
    • Baltscheffsky, M.1    Baltscheffsky, H.2    Von Stedingk, L.-V.3
  • 9
    • 0014004370 scopus 로고
    • Inorganic pyrophosphate: Formation in bacterial photophosphorylation
    • Baltscheffsky H., Von Stedingk L.V., Heldt H.W., Klingenberg M. Inorganic pyrophosphate: formation in bacterial photophosphorylation. Science. 153:1966;1120-1122
    • (1966) Science , vol.153 , pp. 1120-1122
    • Baltscheffsky, H.1    Von Stedingk, L.V.2    Heldt, H.W.3    Klingenberg, M.4
  • 10
    • 0026512325 scopus 로고
    • Molecular cloning and sequence of cDNA encoding the pyrophosphate- energized vacuolar membrane proton pump of Arabidopsis thaliana
    • Sarafian V., Kim Y., Poole R.J., Rea P.A. Molecular cloning and sequence of cDNA encoding the pyrophosphate-energized vacuolar membrane proton pump of Arabidopsis thaliana. Proc. Natl. Acad. Sci. U. S. A. 89:1992;1775-1779
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 1775-1779
    • Sarafian, V.1    Kim, Y.2    Poole, R.J.3    Rea, P.A.4
  • 11
    • 0031806558 scopus 로고    scopus 로고
    • A pyrophosphate synthase gene: Molecular cloning and sequencing of the cDNA encoding the inorganic pyrophosphate synthase from Rhodospirillum rubrum
    • Baltscheffsky M., Nadanaciva S., Schultz A. A pyrophosphate synthase gene: molecular cloning and sequencing of the cDNA encoding the inorganic pyrophosphate synthase from Rhodospirillum rubrum. Biochim. Biophys. Acta. 1364:1998;301-306
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 301-306
    • Baltscheffsky, M.1    Nadanaciva, S.2    Schultz, A.3
  • 12
    • 0037151064 scopus 로고    scopus 로고
    • +-pyrophosphatase of Rhodospirillum rubrum: High-yield expression in Escherichia coli and identification of the cys residues responsible for inactivation by mersalyl
    • +-pyrophosphatase of Rhodospirillum rubrum: high-yield expression in Escherichia coli and identification of the cys residues responsible for inactivation by mersalyl. J. Biol. Chem. 277:2002;22209-22214
    • (2002) J. Biol. Chem. , vol.277 , pp. 22209-22214
    • Belogurov, G.A.1    Turkina, M.V.2    Penttinen, A.3    Huopalahti, S.4    Baykov, A.A.5    Lahti, R.6
  • 14
    • 2642569586 scopus 로고
    • Evolutionary and mechanistic aspects on coupling and phosphorylation in photosynthetic bacteria
    • Barber J. Amsterdam: Elsevier
    • Baltscheffsky M., Baltscheffsky H., Boork J. Evolutionary and mechanistic aspects on coupling and phosphorylation in photosynthetic bacteria. Barber J. Topics in Photosynthesis. vol. 4:1982;249-272 Elsevier, Amsterdam
    • (1982) Topics in Photosynthesis , vol.4 , pp. 249-272
    • Baltscheffsky, M.1    Baltscheffsky, H.2    Boork, J.3
  • 15
    • 0030868387 scopus 로고    scopus 로고
    • +-pyrophosphatase by N,N′- dicyclohexylcarbodiimide
    • +-pyrophosphatase by N, N′-dicyclohexylcarbodiimide. J. Biol. Chem. 272:1997;22340-22348
    • (1997) J. Biol. Chem. , vol.272 , pp. 22340-22348
    • Zhen, R.G.1    Kim, E.J.2    Rea, P.A.3
  • 17
    • 0020674637 scopus 로고
    • 2+ pump studied by irreversible modification with fluorescein isothiocyanate
    • 2+ pump studied by irreversible modification with fluorescein isothiocyanate. J. Biol. Chem. 258:1983;169-175
    • (1983) J. Biol. Chem. , vol.258 , pp. 169-175
    • Muallem, S.1    Karlish, S.J.D.2
  • 19
    • 0017632673 scopus 로고
    • Modification of histidyl residues in proteins by diethylpyrocarbonate
    • Miles E.W. Modification of histidyl residues in proteins by diethylpyrocarbonate. Methods Enzymol. 47:1977;431-442
    • (1977) Methods Enzymol. , vol.47 , pp. 431-442
    • Miles, E.W.1
  • 21
    • 77956908706 scopus 로고
    • Phospholipases
    • Boyer P.D. New York: Academic Press
    • Dennis E.A. Phospholipases. Boyer P.D. The Enzymes. vol. XVI:1983;307-353 Academic Press, New York
    • (1983) The Enzymes , vol.16 , pp. 307-353
    • Dennis, E.A.1
  • 22
    • 0034636122 scopus 로고    scopus 로고
    • Lipases provide a new mechanistic model for polyhydroxybutyrate (PHB) synthases: Characterization of the functional residues in Chromatium vinosum PHB synthase
    • Jia Y., Kappock T.J., Frick T., Sinskey A.J., Stubbe J. Lipases provide a new mechanistic model for polyhydroxybutyrate (PHB) synthases: characterization of the functional residues in Chromatium vinosum PHB synthase. Biochemistry. 39:2000;3927-3936
    • (2000) Biochemistry , vol.39 , pp. 3927-3936
    • Jia, Y.1    Kappock, T.J.2    Frick, T.3    Sinskey, A.J.4    Stubbe, J.5
  • 23
    • 0035252801 scopus 로고    scopus 로고
    • Molecular dynamics study of active-site interactions with tetracoordinate transients in acetylcholinesterase and its mutants
    • Enyedy I.J., Kovach I.M., Bencsura A. Molecular dynamics study of active-site interactions with tetracoordinate transients in acetylcholinesterase and its mutants. Biochem. J. 353:2001;645-653
    • (2001) Biochem. J. , vol.353 , pp. 645-653
    • Enyedy, I.J.1    Kovach, I.M.2    Bencsura, A.3
  • 24
    • 0031283056 scopus 로고    scopus 로고
    • Histidine→carboxamide ligand substitutions in the zinc binding site of carbonic anhydrase II alter metal coordination geometry but retain catalytic activity
    • Lesburg C.A., Huang C., Christianson D.W., Fierke C.A. Histidine→carboxamide ligand substitutions in the zinc binding site of carbonic anhydrase II alter metal coordination geometry but retain catalytic activity. Biochemistry. 36:1997;15780-15791
    • (1997) Biochemistry , vol.36 , pp. 15780-15791
    • Lesburg, C.A.1    Huang, C.2    Christianson, D.W.3    Fierke, C.A.4
  • 26
    • 0035798394 scopus 로고    scopus 로고
    • The "open" and "closed" structures of the type-C inorganic pyrophosphatase from Bacillus subtilis and Streptococcus gordonii
    • Ahn S., Milner A.J., Fütterer K., Konopka M., Ilias M., Young T.W., White S.A. The "open" and "closed" structures of the type-C inorganic pyrophosphatase from Bacillus subtilis and Streptococcus gordonii. J. Mol. Biol. 313:2001;797-811
    • (2001) J. Mol. Biol. , vol.313 , pp. 797-811
    • Ahn, S.1    Milner, A.J.2    Fütterer, K.3    Konopka, M.4    Ilias, M.5    Young, T.W.6    White, S.A.7
  • 28
    • 0030593468 scopus 로고    scopus 로고
    • Overproduction of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B., Walker J.E. Overproduction of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260:1996;289-298
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 30
    • 0035941484 scopus 로고    scopus 로고
    • Codon bias at the 3′-side of the initiation codon is correlated with translation initiation efficiency in Escherichia coli
    • Stenström C.M., Jin H., Major L.L., Tate W.P., Isaksson L.A. Codon bias at the 3′-side of the initiation codon is correlated with translation initiation efficiency in Escherichia coli. Gene. 263:2001;273-284
    • (2001) Gene , vol.263 , pp. 273-284
    • Stenström, C.M.1    Jin, H.2    Major, L.L.3    Tate, W.P.4    Isaksson, L.A.5
  • 31
    • 0025752365 scopus 로고
    • Proton-pumping N,N′-dicyclohexylcarbodiimide-sensitive inorganic pyrophosphate synthase from Rhodospirillum rubrum: Purification, characterization, and reconstitution
    • Nyrén P., Nore B.F., Strid Å. Proton-pumping N, N′-dicyclohexylcarbodiimide-sensitive inorganic pyrophosphate synthase from Rhodospirillum rubrum: purification, characterization, and reconstitution. Biochemistry. 30:1991;2883-2887
    • (1991) Biochemistry , vol.30 , pp. 2883-2887
    • Nyrén, P.1    Nore, B.F.2    Strid, Å.3
  • 32
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 0014663389 scopus 로고
    • Estimation of enzymatically produced orthophosphate in the presence of cysteine and adenosine triphosphate
    • Rathbun W.B., Betlach V.M. Estimation of enzymatically produced orthophosphate in the presence of cysteine and adenosine triphosphate. Anal. Biochem. 28:1969;436-445
    • (1969) Anal. Biochem. , vol.28 , pp. 436-445
    • Rathbun, W.B.1    Betlach, V.M.2
  • 34
    • 0011599499 scopus 로고
    • Tonoplast adenosine triphosphatase and inorganic pyrophosphatase
    • Rea P.A., Turner J.C. Tonoplast adenosine triphosphatase and inorganic pyrophosphatase. Methods Plant Biochem. 3:1990;385-405
    • (1990) Methods Plant Biochem. , vol.3 , pp. 385-405
    • Rea, P.A.1    Turner, J.C.2
  • 36
    • 0029833537 scopus 로고    scopus 로고
    • PH-induced proton permeability changes of plasma membrane vesicles
    • Miedema H., Staal M., Prins H.B.A. pH-induced proton permeability changes of plasma membrane vesicles. J. Membr. Biol. 152:1996;159-167
    • (1996) J. Membr. Biol. , vol.152 , pp. 159-167
    • Miedema, H.1    Staal, M.2    Prins, H.B.A.3
  • 38
    • 0000399944 scopus 로고
    • Inactivation of myosin by 2,4-dinitrophenol and protection by adenosine triphosphate and other phosphate compounds
    • Levy H.M., Leber P.D., Ryan E.M. Inactivation of myosin by 2, 4-dinitrophenol and protection by adenosine triphosphate and other phosphate compounds. J. Biol. Chem. 238:1963;3654-3659
    • (1963) J. Biol. Chem. , vol.238 , pp. 3654-3659
    • Levy, H.M.1    Leber, P.D.2    Ryan, E.M.3
  • 41
    • 0035900017 scopus 로고    scopus 로고
    • Malonyl-CoA: ACP transacylase from Streptomyces coelicolor has two alternative catalytically active nucleophiles
    • Dreier J., Li Q., Khosla C. Malonyl-CoA: ACP transacylase from Streptomyces coelicolor has two alternative catalytically active nucleophiles. Biochemistry. 40:2001;12407-12411
    • (2001) Biochemistry , vol.40 , pp. 12407-12411
    • Dreier, J.1    Li, Q.2    Khosla, C.3
  • 42
    • 0033581166 scopus 로고    scopus 로고
    • Manganese as a replacement for magnesium and zinc: Functional comparisons of the divalent ions
    • Bock C.W., Katz A.K., Markham G.D., Glusker J.P. Manganese as a replacement for magnesium and zinc: functional comparisons of the divalent ions. J. Am. Chem. Soc. 121:1999;7360-7372
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 7360-7372
    • Bock, C.W.1    Katz, A.K.2    Markham, G.D.3    Glusker, J.P.4
  • 45
    • 0037147233 scopus 로고    scopus 로고
    • +-pyrophosphatase in Carboxydothermus hydrogenoformans
    • +-pyrophosphatase in Carboxydothermus hydrogenoformans. J. Biol. Chem. 277:2002;49651-49654
    • (2002) J. Biol. Chem. , vol.277 , pp. 49651-49654
    • Belogurov, G.A.1    Lahti, R.2


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