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Volumn 237, Issue 1, 1996, Pages 247-254

Escherichia coli isocitrate dehydrogenase kinase/phosphatase Overproduction and kinetics of interaction with its substrates by using intrinsic fluorescence and fluorescent nucleotide analogues

Author keywords

ATP analogs; Fluorescent nucleotides; Intrinsic fluorescence; Isocitrate dehydrogenase kinase phosphatase; Nucleotide binding protein

Indexed keywords

ADENOSINE DERIVATIVE; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; ISOCITRATE DEHYDROGENASE; NUCLEOTIDE;

EID: 0030010395     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0247n.x     Document Type: Article
Times cited : (16)

References (39)
  • 1
    • 0013894468 scopus 로고
    • The role and control of the glyoxylate shunt in Escherichia coli
    • Kornberg, H. L. (1966) The role and control of the glyoxylate shunt in Escherichia coli, Biochem. J. 99, 1-11.
    • (1966) Biochem. J. , vol.99 , pp. 1-11
    • Kornberg, H.L.1
  • 2
    • 0017872760 scopus 로고
    • Acetate metabolism in Escherichia coli
    • Lakshmi, T. & Helling, R. (1978) Acetate metabolism in Escherichia coli, Can. J. Microbiol. 24, 149-153.
    • (1978) Can. J. Microbiol. , vol.24 , pp. 149-153
    • Lakshmi, T.1    Helling, R.2
  • 3
    • 0021767546 scopus 로고
    • Amino acid sequence round the site of phosphorylation in isocitrate dehydrogenase from Escherichia coli ML308
    • Borthwick, A. C., Holms, W. H. & Nimmo, H. G. (1984) Amino acid sequence round the site of phosphorylation in isocitrate dehydrogenase from Escherichia coli ML308, FEBS Lett. 174, 112-115.
    • (1984) FEBS Lett. , vol.174 , pp. 112-115
    • Borthwick, A.C.1    Holms, W.H.2    Nimmo, H.G.3
  • 4
    • 0018397107 scopus 로고
    • Phosphorylation of isocitrate dehydrogenase of Escherichia coli
    • Garnak, M. & Reeves, H. C. (1978) Phosphorylation of isocitrate dehydrogenase of Escherichia coli, Science 203, 1111-1112.
    • (1978) Science , vol.203 , pp. 1111-1112
    • Garnak, M.1    Reeves, H.C.2
  • 5
    • 0023750782 scopus 로고
    • Nucleotide sequence and expression of the aceK gene coding for isocitrate dehydrogenase kinase/phosphatase in Escherichia coli
    • Cortay, J. C., Bleicher, F., Rieul, C., Reeves, H. C. & Cozzone, A. J. (1988) Nucleotide sequence and expression of the aceK gene coding for isocitrate dehydrogenase kinase/phosphatase in Escherichia coli, J. Bacteriol. 170, 89-97.
    • (1988) J. Bacteriol. , vol.170 , pp. 89-97
    • Cortay, J.C.1    Bleicher, F.2    Rieul, C.3    Reeves, H.C.4    Cozzone, A.J.5
  • 6
    • 0020355238 scopus 로고
    • A protein with kinase and phosphatase activities involved in regulation of tricarboxylic acid cycle
    • LaPorte, D. C. & Koshland, D. E. Jr (1982) A protein with kinase and phosphatase activities involved in regulation of tricarboxylic acid cycle, Nature 300, 458-460.
    • (1982) Nature , vol.300 , pp. 458-460
    • LaPorte, D.C.1    Koshland Jr., D.E.2
  • 7
    • 0022392412 scopus 로고
    • A single gene codes for the kinase and phosphatase which regulate isocitrate dehydrogenase
    • LaPorte, D. C. & Chung, T. (1985) A single gene codes for the kinase and phosphatase which regulate isocitrate dehydrogenase, J. Biol. Chem. 260, 15291-15297.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15291-15297
    • LaPorte, D.C.1    Chung, T.2
  • 8
    • 0023645302 scopus 로고
    • Inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate
    • Thorsness, P. E. & Koshland, D. E. Jr (1987) Inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate, J. Biol. Chem. 262, 10422-10425.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10422-10425
    • Thorsness, P.E.1    Koshland Jr., D.E.2
  • 9
    • 0023665375 scopus 로고
    • Isocitrate dehydrogenase kinase/phosphatase exhibits an intrinsic adenosine triphosphatase activity
    • Stueland, C. S., Eck, K. R., Stiglhauer, K. T. & LaPorte, D. C. (1987) Isocitrate dehydrogenase kinase/phosphatase exhibits an intrinsic adenosine triphosphatase activity, J. Biol. Chem. 262, 16095-16099.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16095-16099
    • Stueland, C.S.1    Eck, K.R.2    Stiglhauer, K.T.3    LaPorte, D.C.4
  • 10
    • 0020592357 scopus 로고
    • Phosphorylation of isocitrate dehydrogenase as a demonstration of enhanced sensitivity in covalent regulation
    • LaPorte, D. C. & Koshland, D. E. Jr (1983) Phosphorylation of isocitrate dehydrogenase as a demonstration of enhanced sensitivity in covalent regulation, Nature 305, 286-290.
    • (1983) Nature , vol.305 , pp. 286-290
    • LaPorte, D.C.1    Koshland Jr., D.E.2
  • 11
    • 0021451715 scopus 로고
    • The regulatory properties of isocitrate dehydrogenase kinase and isocitrate dehydrogenase phosphatase from Escherichia coli and the role of these activities in the control of isocitrate dehydrogenase
    • Nimmo, G. A. & Nimmo, H. G. (1984) The regulatory properties of isocitrate dehydrogenase kinase and isocitrate dehydrogenase phosphatase from Escherichia coli and the role of these activities in the control of isocitrate dehydrogenase, Eur. J. Biochem. 141, 409-414.
    • (1984) Eur. J. Biochem. , vol.141 , pp. 409-414
    • Nimmo, G.A.1    Nimmo, H.G.2
  • 12
    • 0021741048 scopus 로고
    • The branch point effect. Ultrasensitivity and subsensitivity to metabolic control
    • LaPorte, D. C., Walsh, K. & Koshland, D. E. Jr (1984) The branch point effect. Ultrasensitivity and subsensitivity to metabolic control, J. Biol. Chem. 259, 14068-14075.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14068-14075
    • LaPorte, D.C.1    Walsh, K.2    Koshland Jr., D.E.3
  • 13
    • 0023819835 scopus 로고
    • Photoaffinity labelling shows that Escherichia coli isocitrate dehydrogenase kinase/phosphatase contains a single ATP-binding site
    • Valera, I. & Nimmo, H. G. (1988) Photoaffinity labelling shows that Escherichia coli isocitrate dehydrogenase kinase/phosphatase contains a single ATP-binding site, FEBS Lett. 231, 361-365.
    • (1988) FEBS Lett. , vol.231 , pp. 361-365
    • Valera, I.1    Nimmo, H.G.2
  • 14
    • 0024024834 scopus 로고
    • Nucleotide sequence of aceK, the gene encoding isocitrate dehydrogenase kinase/phosphatase
    • Klumpp, D. J., Plank, D. W., Bowdin, L. D., Stueland, C. S., Chung, T. & LaPorte, D. C. (1988) Nucleotide sequence of aceK, the gene encoding isocitrate dehydrogenase kinase/phosphatase, J. Bacteriol. 170, 2763-2769.
    • (1988) J. Bacteriol. , vol.170 , pp. 2763-2769
    • Klumpp, D.J.1    Plank, D.W.2    Bowdin, L.D.3    Stueland, C.S.4    Chung, T.5    LaPorte, D.C.6
  • 15
    • 0024405978 scopus 로고
    • Mutation of the predicted ATP binding site inactivates both activities of isocitrate dehydrogenase kinase/phosphatase
    • Stueland, C. S., Ikeda, T. P. & LaPorte, D. C. (1989) Mutation of the predicted ATP binding site inactivates both activities of isocitrate dehydrogenase kinase/phosphatase, J. Biol. Chem. 264, 13775-13779.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13775-13779
    • Stueland, C.S.1    Ikeda, T.P.2    LaPorte, D.C.3
  • 17
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanish-Perron, C., Viera, J. & Messing, J. (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors, Gene 33, 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanish-Perron, C.1    Viera, J.2    Messing, J.3
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0028239937 scopus 로고
    • In vitro asymetric binding of the pleiotropic regulatory protein, FruR, to the ace operator controlling glyoxylate shunt enzyme synthesis
    • Cortay, J. C., Nègre, D., Scarabel, M., Ramseier, T. M., Vartak, N. B., Reizer, J. & Cozzone, A. J. (1994) In vitro asymetric binding of the pleiotropic regulatory protein, FruR, to the ace operator controlling glyoxylate shunt enzyme synthesis, J. Biol. Chem. 269, 14885-14891.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14885-14891
    • Cortay, J.C.1    Nègre, D.2    Scarabel, M.3    Ramseier, T.M.4    Vartak, N.B.5    Reizer, J.6    Cozzone, A.J.7
  • 20
    • 0027452330 scopus 로고
    • Glutamine 170 to tyrosine substitution in yeast mitochondrial F1 β-subunit increases catalytic site interaction with GDP and IDP produces negative cooperatively of GTP and ITP hydrolysis
    • Jault, J. M., Divita, G., Allison, W. S. & Di Pietro, A. (1993) Glutamine 170 to tyrosine substitution in yeast mitochondrial F1 β-subunit increases catalytic site interaction with GDP and IDP produces negative cooperatively of GTP and ITP hydrolysis, J. Biol. Chem. 268, 20762-20767.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20762-20767
    • Jault, J.M.1    Divita, G.2    Allison, W.S.3    Di Pietro, A.4
  • 21
    • 0018696727 scopus 로고
    • Purification and properties of phosphorylated isocitrate dehydrogenase of Escherichia coli
    • Garnak, M. & Reeves, H. C. (1979) Purification and properties of phosphorylated isocitrate dehydrogenase of Escherichia coli, J. Biol. Chem. 254, 7915-7920.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7915-7920
    • Garnak, M.1    Reeves, H.C.2
  • 23
    • 0018787718 scopus 로고
    • Synthesis and properties of a new fluorescent analog of ATP: Adenosine-5-triphosphoro-γ-1-(5-sulfonic acid) naphthylamidate
    • Yarbrough, L. R. (1978) Synthesis and properties of a new fluorescent analog of ATP: adenosine-5-triphosphoro-γ-1-(5-sulfonic acid) naphthylamidate, J. Biol. Chem. 254, 12069-12073.
    • (1978) J. Biol. Chem. , vol.254 , pp. 12069-12073
    • Yarbrough, L.R.1
  • 24
    • 0021114740 scopus 로고
    • Penetration of small molecules into proteins studied by quenching of phosphorescence and fluorescence
    • Calhoun, D. B., Vanderkooi, J. M. & Englander, S. W. (1983) Penetration of small molecules into proteins studied by quenching of phosphorescence and fluorescence, Biochemistry 22, 1533-1539.
    • (1983) Biochemistry , vol.22 , pp. 1533-1539
    • Calhoun, D.B.1    Vanderkooi, J.M.2    Englander, S.W.3
  • 25
    • 0017288499 scopus 로고
    • Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies
    • Eftink, M. R. & Ghiron, C. A. (1976) Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies, Biochemistry 15, 672-680.
    • (1976) Biochemistry , vol.15 , pp. 672-680
    • Eftink, M.R.1    Ghiron, C.A.2
  • 26
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and lysozyme by iodide ions
    • Lehrer, S. S. (1971) Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and lysozyme by iodide ions, Biochemistry 10, 3254-3262.
    • (1971) Biochemistry , vol.10 , pp. 3254-3262
    • Lehrer, S.S.1
  • 27
    • 0026603594 scopus 로고
    • Single-step purification of bacterially expressed polypeptides containing an oligo-histidine domain
    • Van Dyke, M. W., Sirito, M. & Sawadogo, M. (1992) Single-step purification of bacterially expressed polypeptides containing an oligo-histidine domain, Gene III, 99-104.
    • (1992) Gene , vol.3 , pp. 99-104
    • Van Dyke, M.W.1    Sirito, M.2    Sawadogo, M.3
  • 28
    • 0023659137 scopus 로고
    • New metal chelate adsorbents selective for proteins and peptide containing neighbouring histidine residues
    • Hochuli, E., Döbeli, H. & Schacher, A. (1987) New metal chelate adsorbents selective for proteins and peptide containing neighbouring histidine residues, J. Chromatogr. 411, 177-184.
    • (1987) J. Chromatogr. , vol.411 , pp. 177-184
    • Hochuli, E.1    Döbeli, H.2    Schacher, A.3
  • 29
    • 0021448708 scopus 로고
    • Partial purification and properties of isocitrate dehydrogenase kinase/phosphatase from Escherichia coli ML308
    • Ninimo, G. A., Borthwick, A. C., Holms, W. H. & Nimmo, H. G. (1984) Partial purification and properties of isocitrate dehydrogenase kinase/phosphatase from Escherichia coli ML308, Eur. J. Biochem. 141, 401-408.
    • (1984) Eur. J. Biochem. , vol.141 , pp. 401-408
    • Ninimo, G.A.1    Borthwick, A.C.2    Holms, W.H.3    Nimmo, H.G.4
  • 31
    • 0015794613 scopus 로고
    • Fluorescence and the location of tryptophan residues in protein molecules
    • Burstein, E. A., Vedenkina, N. S. & Ivkova, M. N. (1973) Fluorescence and the location of tryptophan residues in protein molecules, Photochem. Photobiol. 18, 263-279.
    • (1973) Photochem. Photobiol. , vol.18 , pp. 263-279
    • Burstein, E.A.1    Vedenkina, N.S.2    Ivkova, M.N.3
  • 32
    • 0025929570 scopus 로고
    • Fluorescence techniques for studying protein structure
    • Eftink, M. R. (1991) Fluorescence techniques for studying protein structure, Methods Biochem. Anal. 35, 127-205.
    • (1991) Methods Biochem. Anal. , vol.35 , pp. 127-205
    • Eftink, M.R.1
  • 33
    • 0020674810 scopus 로고
    • New ribose modified fluorescent analogs of adenosine and guanine nucleotides available as substrates for various enzymes
    • Hiratsuka, T. (1983) New ribose modified fluorescent analogs of adenosine and guanine nucleotides available as substrates for various enzymes, Biochim. Biophys. Acta 742, 496-508.
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 496-508
    • Hiratsuka, T.1
  • 35
    • 0026018966 scopus 로고
    • Kinetics of 2′(3′)-O-(N-methylanthraniloyl)-ATP with myosin subfragment I and actomyosin subfragment I: Characterization of two acto. S1. ADP complexes
    • Woodward, S. K. A., Eccleston, J. F. & Geeves, M. A. (1991) Kinetics of 2′(3′)-O-(N-methylanthraniloyl)-ATP with myosin subfragment I and actomyosin subfragment I: characterization of two acto. S1. ADP complexes, Biochemistry 30, 422-430.
    • (1991) Biochemistry , vol.30 , pp. 422-430
    • Woodward, S.K.A.1    Eccleston, J.F.2    Geeves, M.A.3
  • 36
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks, S. K., Quinn, A. M. & Hunter, T. (1988) The protein kinase family: conserved features and deduced phylogeny of the catalytic domains, Science 241, 42-52.
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 37
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D. R., Zheng, J., Ten Eyck, L. F., Ashford, V. A., Xuong, N. H., Taylor, S. S. & Sowadski, J. M. (1991) Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase, Science 253, 407-414.
    • (1991) Science , vol.253 , pp. 407-414
    • Knighton, D.R.1    Zheng, J.2    Ten Eyck, L.F.3    Ashford, V.A.4    Xuong, N.H.5    Taylor, S.S.6    Sowadski, J.M.7
  • 39
    • 0028157664 scopus 로고
    • Atomic structure of the MAP kinase ERK2 at 2.3 Å
    • Zhang, F., Strand, A., Robbins, D., Cobb, M. H. & Goldsmith, E. (1994) Atomic structure of the MAP kinase ERK2 at 2.3 Å, Nature 367, 704-711.
    • (1994) Nature , vol.367 , pp. 704-711
    • Zhang, F.1    Strand, A.2    Robbins, D.3    Cobb, M.H.4    Goldsmith, E.5


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