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Volumn 1608, Issue 2-3, 2004, Pages 190-199

Roles of histidine residues in plant vacuolar H+-pyrophosphatase

Author keywords

H+ pyrophosphatase; Histidine; Proton translocation; Tonoplast; Vacuole

Indexed keywords

ALANINE; DIETHYL PYROCARBONATE; HISTIDINE; INORGANIC PYROPHOSPHATASE; POTASSIUM ION; PROTON; TRYPSIN;

EID: 1042267380     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2004.01.001     Document Type: Article
Times cited : (28)

References (40)
  • 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
  • 5
    • 0000969470 scopus 로고    scopus 로고
    • +-pumping inorganic pyrophosphatase, (studies using ligand protection from covalent inhibitors)
    • +-pumping inorganic pyrophosphatase, (studies using ligand protection from covalent inhibitors). Plant Physiol. 111:1996;195-202.
    • (1996) Plant Physiol. , vol.111 , pp. 195-202
    • Gordon-Weeks, R.1    Steele, S.H.2    Leigh, R.A.3
  • 6
    • 0000703574 scopus 로고
    • 2+-dependent, cation-stimulated inorganic pyrophosphatase associated with vacuoles isolated from storage roots of red beet (Beta vulgaris L.)
    • 2+-dependent, cation-stimulated inorganic pyrophosphatase associated with vacuoles isolated from storage roots of red beet (Beta vulgaris L.). Planta. 153:1981;150-155.
    • (1981) Planta , vol.153 , pp. 150-155
    • Walker, R.R.1    Leigh, R.A.2
  • 7
    • 0026071909 scopus 로고
    • 2+ and immunological comparison with other inorganic pyrophosphatases
    • 2+ and immunological comparison with other inorganic pyrophosphatases. Eur. J. Biochem. 196:1991;11-17.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 11-17
    • Maeshima, M.1
  • 8
    • 0027219384 scopus 로고
    • Differential sensitivity of membrane-associated pyrophosphatases to inhibition by diphosphonates and fluoride delineates two classes of enzyme
    • Baykov A.A., Dubnova E.B., Bakuleva N.P., Evtushenko O.A., Zhen R.-G., Rea P.A. Differential sensitivity of membrane-associated pyrophosphatases to inhibition by diphosphonates and fluoride delineates two classes of enzyme. FEBS Lett. 327:1993;199-202.
    • (1993) FEBS Lett. , vol.327 , pp. 199-202
    • Baykov, A.A.1    Dubnova, E.B.2    Bakuleva, N.P.3    Evtushenko, O.A.4    Zhen, R.-G.5    Rea, P.A.6
  • 11
    • 0000127303 scopus 로고
    • An essential arginyl residue in the tonoplast pyrophosphatase from etiolated mung bean seedlings
    • Kuo S.Y., Pan R.L. An essential arginyl residue in the tonoplast pyrophosphatase from etiolated mung bean seedlings. Plant Physiol. 93:1990;1128-1133.
    • (1990) Plant Physiol. , vol.93 , pp. 1128-1133
    • Kuo, S.Y.1    Pan, R.L.2
  • 13
    • 0028893719 scopus 로고
    • 634 for inhibition by maleimides but not catalysis
    • 634 for inhibition by maleimides but not catalysis. J. Biol. Chem. 270:1995;2630-2635.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2630-2635
    • Kim, E.J.1    Zhen, R.-G.2    Rea, P.A.3
  • 17
    • 0030868387 scopus 로고    scopus 로고
    • +-pyrophosphatase by N,N′- dicyclohexylcarbodi-imide
    • +-pyrophosphatase by N,N′-dicyclohexylcarbodi-imide. 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
  • 19
    • 0029858086 scopus 로고    scopus 로고
    • The role of conserved histidine residues in the pyridine nucleotide transhydrogenase of Escherichia coli
    • Bragg P.D., Hou C. The role of conserved histidine residues in the pyridine nucleotide transhydrogenase of Escherichia coli. Eur. J. Biochem. 241:1996;611-618.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 611-618
    • Bragg, P.D.1    Hou, C.2
  • 20
    • 0032488633 scopus 로고    scopus 로고
    • +-transport by uncoupling protein (UCP-1) is dependent on a histidine pair, absent in UCP-2 and UCP-3
    • +-transport by uncoupling protein (UCP-1) is dependent on a histidine pair, absent in UCP-2 and UCP-3. Biochemistry. 37:1998;3-8.
    • (1998) Biochemistry , vol.37 , pp. 3-8
    • Bienengraeber, M.1    Echtay, K.S.2    Klingenberg, M.3
  • 21
    • 0034640452 scopus 로고    scopus 로고
    • Mechanism of proton translocation by cytochrome c oxidase: A new four-stroke histidine cycle
    • Wikström M. Mechanism of proton translocation by cytochrome c oxidase: a new four-stroke histidine cycle. Biochim. Biophys. Acta. 1458:2000;188-198.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 188-198
    • Wikström, M.1
  • 23
    • 0028048581 scopus 로고
    • +)-coupled glutamate transporter from rat brain
    • +)-coupled glutamate transporter from rat brain. J. Biol. Chem. 269:1994;19573-19577.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19573-19577
    • Zhang, Y.1    Pines, G.2    Kanner, B.I.3
  • 24
    • 0035918599 scopus 로고    scopus 로고
    • Protonation of histidine and histidine-tryptophan interaction in the activation of the M2 ion channel from influenza a virus
    • Okada A., Miura T., Takeuchi H. Protonation of histidine and histidine-tryptophan interaction in the activation of the M2 ion channel from influenza A virus. Biochemistry. 40:2001;6053-6060.
    • (2001) Biochemistry , vol.40 , pp. 6053-6060
    • Okada, A.1    Miura, T.2    Takeuchi, H.3
  • 29
    • 0028278224 scopus 로고
    • Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of the substrate-binding subunit for proton transport
    • Kim E.J., Zhen R.-G., Rea P.A. Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of the substrate-binding subunit for proton transport. Proc. Natl. Acad. Sci. U. S. A. 91:1994;6128-6132.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 6128-6132
    • Kim, E.J.1    Zhen, R.-G.2    Rea, P.A.3
  • 30
    • 0028954118 scopus 로고
    • Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure
    • Gietz R.D., Schiestl R.H., Willems A.R., Woods R.A. Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast. 11:1995;355-360.
    • (1995) Yeast , vol.11 , pp. 355-360
    • Gietz, R.D.1    Schiestl, R.H.2    Willems, A.R.3    Woods, R.A.4
  • 31
    • 0000715366 scopus 로고
    • Site-directed mutagenesis by double polymerase chain reaction: Megaprimer method
    • White B.A. New Jersey: Humana Press
    • Barik S. Site-directed mutagenesis by double polymerase chain reaction: megaprimer method. White B.A. Methods of Molecular Biology. vol. 15: 1993;277-286 Humana Press, New Jersey.
    • (1993) Methods of Molecular Biology , vol.15 , pp. 277-286
    • Barik, S.1
  • 32
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorous
    • Fiske C.H., Subbarow Y. The colorimetric determination of phosphorous. J. Biol. Chem. 66:1925;378-400.
    • (1925) J. Biol. Chem. , vol.66 , pp. 378-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 34
    • 0022485196 scopus 로고
    • Artificial reductant enhancement of the Lowry method for protein determination
    • Larson E., Howlett B., Jagendorf A.T. Artificial reductant enhancement of the Lowry method for protein determination. Anal. Biochem. 155:1986;243-248.
    • (1986) Anal. Biochem. , vol.155 , pp. 243-248
    • Larson, E.1    Howlett, B.2    Jagendorf, A.T.3
  • 36
    • 0037147233 scopus 로고    scopus 로고
    • +-pyrophosphatase of Carboxydothermus hydrogenoformans
    • +-pyrophosphatase of 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
  • 38
    • 0032725586 scopus 로고    scopus 로고
    • A thermostable vacuolar-type membrane pyrophosphatase from the archaeon Pyrobaculum aerophilum: Implications for the origins of pyrophosphate-energized pumps
    • Drozdowicz Y.M., Lu Y.P., Patel V., Fitz-Gibbon S., Miller J.H., Rea P.A. A thermostable vacuolar-type membrane pyrophosphatase from the archaeon Pyrobaculum aerophilum: implications for the origins of pyrophosphate-energized pumps. FEBS Lett. 460:1999;505-512.
    • (1999) FEBS Lett. , vol.460 , pp. 505-512
    • Drozdowicz, Y.M.1    Lu, Y.P.2    Patel, V.3    Fitz-Gibbon, S.4    Miller, J.H.5    Rea, P.A.6
  • 39
    • 0000278261 scopus 로고
    • +-translocating adenosine triphosphatase and pyrophosphatase associated with the tonoplast of Chara coralline
    • +-translocating adenosine triphosphatase and pyrophosphatase associated with the tonoplast of Chara coralline. Plant Cell Physiol. 29:1988;649-657.
    • (1988) Plant Cell Physiol. , vol.29 , pp. 649-657
    • Takeshiga, K.1    Hager, A.2
  • 40
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.