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Volumn 123, Issue 1, 1998, Pages 169-174

Fluorescein 5'-isothiocyanate-modified Na+,K+-ATPase, at Lys-501 of the α-chain, accepts ATP independent of pyridoxal 51-diphospho-5'-adenosine modification at Lys-480

Author keywords

ATP binding; Conformation change; Fluorescein; K+ ATPase; Na+; Pyridoxal

Indexed keywords

ADENOSINE DERIVATIVE; ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATE; FLUORESCEIN ISOTHIOCYANATE; LYSINE; PYRIDOXAL 5 PHOSPHATE;

EID: 0031890075     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021906     Document Type: Article
Times cited : (15)

References (50)
  • 1
    • 85025408146 scopus 로고
    • Flexibility of an active center in sodium-plus-potassium adenosine triphosphatase
    • Post, R.L., Kume, S., Tobin, T., Orcutt, B., and Sen, A.K. (1969) Flexibility of an active center in sodium-plus-potassium adenosine triphosphatase. J. Gen. Physiol. 54, 306S-326S
    • (1969) J. Gen. Physiol. , vol.54
    • Post, R.L.1    Kume, S.2    Tobin, T.3    Orcutt, B.4    Sen, A.K.5
  • 2
    • 0001089662 scopus 로고
    • The (sodium plus potassium)-transport ATPase
    • Martonossi, A., ed. Plenum Publishing, New York
    • Albers, R.W. (1976) The (sodium plus potassium)-transport ATPase in The Enzymes of Biological Membranes (Martonossi, A., ed.) Vol. 3, pp. 283-301, Plenum Publishing, New York
    • (1976) The Enzymes of Biological Membranes , vol.3 , pp. 283-301
    • Albers, R.W.1
  • 3
    • 0002591052 scopus 로고
    • +-transporting adenosine triphosphatase
    • Martonossi, A., ed. Plenum Publishing, New York
    • +-transporting adenosine triphosphatase in The Enzymes of Biological Membranes (Martonossi, A., ed.) Vol. 3, pp. 35-114, Plenum Publishing, New York
    • (1985) The Enzymes of Biological Membranes , vol.3 , pp. 35-114
    • Glynn, I.M.1
  • 5
    • 0015523849 scopus 로고
    • Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase
    • Post, R.L., Hegyvary, C., and Kume, S. (1972) Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase. J. Biol. Chem. 247, 6530-6540
    • (1972) J. Biol. Chem. , vol.247 , pp. 6530-6540
    • Post, R.L.1    Hegyvary, C.2    Kume, S.3
  • 6
    • 0020002086 scopus 로고
    • Occlusion of rubidium ions by the sodium-potassium pump: Its implications for the mechanism of potassium transport
    • Glynn, I.M. and Richards, D.E. (1982) Occlusion of rubidium ions by the sodium-potassium pump: its implications for the mechanism of potassium transport. J. Physiol. 330, 17-43
    • (1982) J. Physiol. , vol.330 , pp. 17-43
    • Glynn, I.M.1    Richards, D.E.2
  • 7
    • 0027404749 scopus 로고
    • Annual review prize lecture. "All hands to the sodium pump."
    • Glynn, I.M. (1993) Annual review prize lecture. "All hands to the sodium pump." J. Physiol. 462, 1-30
    • (1993) J. Physiol. , vol.462 , pp. 1-30
    • Glynn, I.M.1
  • 10
    • 0020491101 scopus 로고
    • +)-ATPase modified with N-[p-(2-benzimidazolyl)-phenyl]maleimide
    • +)-ATPase modified with N-[p-(2-benzimidazolyl)-phenyl]maleimide. J. Biol. Chem. 257, 10659-10667
    • (1982) J. Biol. Chem. , vol.257 , pp. 10659-10667
    • Taniguchi, K.1    Suzuki, K.2    Iida, S.3
  • 14
    • 0024823960 scopus 로고
    • 2+-transporting ATPase of sarcoplasmic reticulum as revealed by an alteration of the target-site specificity of adenosine triphosphopyridoxal
    • 2+-transporting ATPase of sarcoplasmic reticulum as revealed by an alteration of the target-site specificity of adenosine triphosphopyridoxal. J. Biochem. 106, 1121-1125
    • (1989) J. Biochem. , vol.106 , pp. 1121-1125
    • Yamamoto, H.1    Imamura, Y.2    Tagaya, M.3    Fukui, T.4    Kawakita, M.5
  • 15
    • 0025376029 scopus 로고
    • Lysine 480 is an essential residue in the putative ATP site of lamb kidney (Na,K)-ATPase
    • Hinz, H.R. and Kirley, T.L. (1990) Lysine 480 is an essential residue in the putative ATP site of lamb kidney (Na,K)-ATPase. J. Biol. Chem. 265, 10260-10265
    • (1990) J. Biol. Chem. , vol.265 , pp. 10260-10265
    • Hinz, H.R.1    Kirley, T.L.2
  • 17
    • 0019052331 scopus 로고
    • Characterization of conformational changes in (Na,K) ATPase labeled with fluorescein at the active site
    • Karlish, S.J.D. (1980) Characterization of conformational changes in (Na,K) ATPase labeled with fluorescein at the active site. J. Bioenerg. Biomembr. 12, 111-136
    • (1980) J. Bioenerg. Biomembr. , vol.12 , pp. 111-136
    • Karlish, S.J.D.1
  • 20
    • 0021173423 scopus 로고
    • The amino acid sequence of a fluorescein-labeled peptide from the active site of (Na,K)-ATPase
    • Farley, R.A., Tran, C.M., Carilli, C.T., Hawke, D., and Shively, J.E. (1984) The amino acid sequence of a fluorescein-labeled peptide from the active site of (Na,K)-ATPase. J. Biol. Chem. 259, 9532-9535
    • (1984) J. Biol. Chem. , vol.259 , pp. 9532-9535
    • Farley, R.A.1    Tran, C.M.2    Carilli, C.T.3    Hawke, D.4    Shively, J.E.5
  • 21
    • 0025169857 scopus 로고
    • Chemical modification as an approach to elucidation of sodium pump structure-function relations
    • Pedemonte, C.H. and Kaplan, J.H. (1990) Chemical modification as an approach to elucidation of sodium pump structure-function relations. Am. J. Physiol. 258, C1-C23
    • (1990) Am. J. Physiol. , vol.258
    • Pedemonte, C.H.1    Kaplan, J.H.2
  • 24
    • 0030921059 scopus 로고    scopus 로고
    • +-ATPase and reveal the interaction of two ATP sites during catalysis
    • +-ATPase and reveal the interaction of two ATP sites during catalysis. J. Biol. Chem. 272, 16315-16321
    • (1997) J. Biol. Chem. , vol.272 , pp. 16315-16321
    • Thoenges, D.1    Schoner, W.2
  • 25
    • 0023905892 scopus 로고
    • +)-ATPase: Pertinence of the adenine and fluorescein binding sites
    • +)-ATPase: pertinence of the adenine and fluorescein binding sites. Biochim. Biophys. Acta 953, 26-36
    • (1988) Biochim. Biophys. Acta , vol.953 , pp. 26-36
    • Davis, R.L.1    Robinson, J.D.2
  • 26
    • 0029893954 scopus 로고    scopus 로고
    • Binding of 2′(3′)-O- (2,4,6-trinitrophenyl)ADP to soluble αβ protomers of Na,K-ATPase modified with fluorescein isothiocyanate
    • Ward, D.G. and Cavieres, J.D. (1996) Binding of 2′(3′)-O-(2,4,6-trinitrophenyl)ADP to soluble αβ protomers of Na,K-ATPase modified with fluorescein isothiocyanate. J. Biol. Chem. 271, 12317-12321
    • (1996) J. Biol. Chem. , vol.271 , pp. 12317-12321
    • Ward, D.G.1    Cavieres, J.D.2
  • 28
    • 0023395490 scopus 로고
    • +)-ATPase: On the number of ATP sites of the functional unit
    • +)-ATPase: On the number of ATP sites of the functional unit. J. Bioenerg. Biomembr. 19, 359-374
    • (1987) J. Bioenerg. Biomembr. , vol.19 , pp. 359-374
    • Askari, A.1
  • 29
    • 0024320720 scopus 로고
    • +-ATPase in the αβ-protomer. Determination by low-angle laser light scattering photometry coupled with high-performance gel chromatography for substantially simultaneous measurement of ATPase activity and molecular weight
    • +-ATPase in the αβ-protomer. Determination by low-angle laser light scattering photometry coupled with high-performance gel chromatography for substantially simultaneous measurement of ATPase activity and molecular weight. Biochim. Biophys. Acta 983, 217-229
    • (1989) Biochim. Biophys. Acta , vol.983 , pp. 217-229
    • Hayashi, Y.1    Mimura, K.2    Matsui, H.3    Takagi, T.4
  • 30
    • 0025868113 scopus 로고
    • +-activated adenosine triphosphatases
    • Kaplan, J.H. and de Weer, P., eds. The Rockefeller University Press, New York
    • +-activated adenosine triphosphatases in The Sodium Pump, Structure, Mechanism and Regulation (Kaplan, J.H. and de Weer, P., eds.) pp. 227-247, The Rockefeller University Press, New York
    • (1991) The Sodium Pump, Structure, Mechanism and Regulation , pp. 227-247
    • Froehlich, J.P.1    Fendler, K.2
  • 31
    • 0025912747 scopus 로고
    • Functional significance of the oligomeric structure of the Na,K-pump from radiation inactivation and ligand binding
    • Kaplan, J.H. and de Weer, P., eds. The Rockefeller University Press, New York
    • Nørby, J.G. and Jensen, J. (1991) Functional significance of the oligomeric structure of the Na,K-pump from radiation inactivation and ligand binding in The Sodium Pump, Structure, Mechanism and Regulation (Kaplan, J.H. and de Weer, P., eds.) pp. 173-188, The Rockefeller University Press, New York
    • (1991) The Sodium Pump, Structure, Mechanism and Regulation , pp. 173-188
    • Nørby, J.G.1    Jensen, J.2
  • 33
    • 0023002974 scopus 로고
    • Affinity labeling of nucleotide-binding sites on kinases and dehydrogenases by pyridoxal 5′-diphospho-5′-adenosine
    • Tamura, J.K., Rakov, R.D., and Cross, R.L. (1986) Affinity labeling of nucleotide-binding sites on kinases and dehydrogenases by pyridoxal 5′-diphospho-5′-adenosine. J. Biol. Chem. 261, 4126-4133
    • (1986) J. Biol. Chem. , vol.261 , pp. 4126-4133
    • Tamura, J.K.1    Rakov, R.D.2    Cross, R.L.3
  • 34
    • 0023298717 scopus 로고
    • +)-ATPase by low-angle laser light scattering coupled with high performance gel chromatography in the presence of sodium dodecyl sulfate
    • +)-ATPase by low-angle laser light scattering coupled with high performance gel chromatography in the presence of sodium dodecyl sulfate. J. Biochem. 101, 805-811
    • (1987) J. Biochem. , vol.101 , pp. 805-811
    • Takagi, T.1    Maezawa, S.2    Hayashi, Y.3
  • 35
    • 0026699314 scopus 로고
    • Leucine dehydrogenase from Bacillus stearothermophilus: Identification of active-site lysine by modification with pyridoxal phosphate
    • Matsuyama, T., Soda, K., Fukui, T., and Tanizawa, K. (1992) Leucine dehydrogenase from Bacillus stearothermophilus: Identification of active-site lysine by modification with pyridoxal phosphate. J. Biochem. 112, 258-265
    • (1992) J. Biochem. , vol.112 , pp. 258-265
    • Matsuyama, T.1    Soda, K.2    Fukui, T.3    Tanizawa, K.4
  • 37
    • 0015032587 scopus 로고
    • Thallium (I) activation of pyruvate kinase
    • Kayne, K.J. (1971) Thallium (I) activation of pyruvate kinase. Arch. Biochem. Biophys. 143, 232-239
    • (1971) Arch. Biochem. Biophys. , vol.143 , pp. 232-239
    • Kayne, K.J.1
  • 40
    • 0015218603 scopus 로고
    • Binding of adenosine triphosphate to sodium and potassium ion-stimulated adenosine triphosphatase
    • Hegyvary, C. and Post, R.L. (1971) Binding of adenosine triphosphate to sodium and potassium ion-stimulated adenosine triphosphatase. J. Biol. Chem. 246, 5234-5240
    • (1971) J. Biol. Chem. , vol.246 , pp. 5234-5240
    • Hegyvary, C.1    Post, R.L.2
  • 41
    • 0026784847 scopus 로고
    • Lysine 480 is not an essential residue for ATP binding or hydrolysis by Na,K-ATPase
    • Wang, K. and Farley, R.A. (1992) Lysine 480 is not an essential residue for ATP binding or hydrolysis by Na,K-ATPase. J. Biol. Chem. 267, 3577-3580
    • (1992) J. Biol. Chem. , vol.267 , pp. 3577-3580
    • Wang, K.1    Farley, R.A.2
  • 43
    • 0021929639 scopus 로고
    • The amino acid sequence of an active site peptide from the H,K-ATPase of gastric mucosa
    • Farley, R.A. and Faller, L. (1985) The amino acid sequence of an active site peptide from the H,K-ATPase of gastric mucosa. J. Biol. Chem. 260, 3899-3901
    • (1985) J. Biol. Chem. , vol.260 , pp. 3899-3901
    • Farley, R.A.1    Faller, L.2
  • 47
    • 0242449209 scopus 로고
    • The structure of a yeast hexokinase monomer and its complexes with substrates at 2.7-Å resolution
    • Fletterick, R.J., Bates, D.J., and Steitz, T.A. (1975) The structure of a yeast hexokinase monomer and its complexes with substrates at 2.7-Å resolution. Proc. Natl. Acad. Sci. USA 72, 38-42
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 38-42
    • Fletterick, R.J.1    Bates, D.J.2    Steitz, T.A.3
  • 48
    • 0015243646 scopus 로고
    • The interaction of tetraiodofluorescein with dogfish muscle lactate dehydrogenase: A chemical and X-ray crystallographic study
    • Wassarman, P.M. and Lentz, P.J., Jr. (1971) The interaction of tetraiodofluorescein with dogfish muscle lactate dehydrogenase: a chemical and X-ray crystallographic study. J. Mol. Biol. 60, 509-522
    • (1971) J. Mol. Biol. , vol.60 , pp. 509-522
    • Wassarman, P.M.1    Lentz Jr., P.J.2
  • 49
    • 77957075821 scopus 로고
    • Stoichiometrical binding of ligands to less than 160 kilodaltons of Na,K-ATPase
    • Matsui, H., Hayashi, Y., Homareda, H., and Taguchi, M. (1983) Stoichiometrical binding of ligands to less than 160 kilodaltons of Na,K-ATPase. Curr. Top. Membr. Transport 19, 141-148
    • (1983) Curr. Top. Membr. Transport , vol.19 , pp. 141-148
    • Matsui, H.1    Hayashi, Y.2    Homareda, H.3    Taguchi, M.4


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