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Volumn 5, Issue 5, 2010, Pages 499-506

Asymmetric allosteric signaling in aspartate transcarbamoylase

Author keywords

[No Author keywords available]

Indexed keywords

7 HYDROXYCOUMARIN 4 YL ETHYLGLYCINE; ADENOSINE TRIPHOSPHATE; ASPARTATE CARBAMOYLTRANSFERASE; CYTIDINE TRIPHOSPHATE; GLYCINE DERIVATIVE; GUANOSINE TRIPHOSPHATE; UNCLASSIFIED DRUG; URIDINE TRIPHOSPHATE;

EID: 77952862482     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb9003207     Document Type: Article
Times cited : (12)

References (31)
  • 1
    • 0028144138 scopus 로고
    • Aspartate transcarbamoylase from Escherichia coli: Activity and regulation
    • Lipscomb, W. N. (1994) Aspartate transcarbamoylase from Escherichia coli: activity and regulation Adv. Enzymol. 68, 67-151
    • (1994) Adv. Enzymol. , vol.68 , pp. 67-151
    • Lipscomb, W.N.1
  • 2
    • 0014216815 scopus 로고
    • The purification of aspartate transcarbamylase of Escherichia coli and separation of its protein subunits
    • Gerhart, J. C. and Holoubek, H. (1967) The purification of aspartate transcarbamylase of Escherichia coli and separation of its protein subunits J. Biol. Chem. 242, 2886-2892
    • (1967) J. Biol. Chem. , vol.242 , pp. 2886-2892
    • Gerhart, J.C.1    Holoubek, H.2
  • 3
    • 0005552966 scopus 로고
    • In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamylase
    • Wild, J. R., Loughrey-Chen, S. J., and Corder, T. S. (1989) In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamylase Proc. Natl. Acad. Sci. U.S.A. 86, 46-50
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 46-50
    • Wild, J.R.1    Loughrey-Chen, S.J.2    Corder, T.S.3
  • 4
    • 0014250308 scopus 로고
    • Allosteric interactions in aspartate transcarbamoylase: Binding of specific ligands to the native enzyme and isolated subunits
    • Changeux, J.-P., Gerhart, J. C., and Schachman, H. K. (1968) Allosteric interactions in aspartate transcarbamoylase: binding of specific ligands to the native enzyme and isolated subunits Biochemistry 7, 531-538
    • (1968) Biochemistry , vol.7 , pp. 531-538
    • Changeux, J.-P.1    Gerhart, J.C.2    Schachman, H.K.3
  • 5
    • 0015937197 scopus 로고
    • Equilibrium binding study of the interaction of aspartate transcarbamoylase with cytidine 5?-triphosphate and adenosine 5?-triphosphate
    • Matsumoto, S. and Hammes, G. G. (1973) Equilibrium binding study of the interaction of aspartate transcarbamoylase with cytidine 5?-triphosphate and adenosine 5?-triphosphate Biochemistry 12, 1388-1394
    • (1973) Biochemistry , vol.12 , pp. 1388-1394
    • Matsumoto, S.1    Hammes, G.G.2
  • 6
    • 0017649170 scopus 로고
    • Asymmetry of binding and physical assignments of CTP and ATP sites in aspartate transcarbamoylase
    • Suter, P. and Rosenbusch, J. P. (1977) Asymmetry of binding and physical assignments of CTP and ATP sites in aspartate transcarbamoylase J. Biol. Chem. 252, 8136-8141
    • (1977) J. Biol. Chem. , vol.252 , pp. 8136-8141
    • Suter, P.1    Rosenbusch, J.P.2
  • 7
    • 0014943828 scopus 로고
    • Binding of cytidine triphosphate to aspartate transcarbamylase
    • Winlund, C. C. and Chamberlin, M. J. (1970) Binding of cytidine triphosphate to aspartate transcarbamylase Biochem. Biophys. Res. Commun. 40, 43-49
    • (1970) Biochem. Biophys. Res. Commun. , vol.40 , pp. 43-49
    • Winlund, C.C.1    Chamberlin, M.J.2
  • 8
    • 0025837016 scopus 로고
    • The synergistic inhibition of Escherichia coli aspartate carbamoyltransferase by UTP in the presence of CTP is due to the binding of UTP to the low affinity CTP sites
    • Zhang, Y. and Kantrowitz, E. R. (1991) The synergistic inhibition of Escherichia coli aspartate carbamoyltransferase by UTP in the presence of CTP is due to the binding of UTP to the low affinity CTP sites J. Biol. Chem. 266, 22154-22158
    • (1991) J. Biol. Chem. , vol.266 , pp. 22154-22158
    • Zhang, Y.1    Kantrowitz, E.R.2
  • 9
    • 0026792903 scopus 로고
    • Synergistic inhibition of Escherichia coli aspartate transcarbamoylase by CTP and UTP: Binding studies using continuous-flow dialysis
    • England, P. and Hervé, G. (1992) Synergistic inhibition of Escherichia coli aspartate transcarbamoylase by CTP and UTP: binding studies using continuous-flow dialysis Biochemistry 31, 9725-9732
    • (1992) Biochemistry , vol.31 , pp. 9725-9732
    • England, P.1    Hervé, G.2
  • 10
    • 0016390542 scopus 로고
    • Nuclear magnetic resonance study of the interaction of inhibitory nucleosides with Escherichia coli aspartate transcarbamylase and its regulatory subunit
    • London, R. E. and Schmidt, P. G. (1974) Nuclear magnetic resonance study of the interaction of inhibitory nucleosides with Escherichia coli aspartate transcarbamylase and its regulatory subunit Biochemistry 13, 1170-1179
    • (1974) Biochemistry , vol.13 , pp. 1170-1179
    • London, R.E.1    Schmidt, P.G.2
  • 11
    • 0019320467 scopus 로고
    • Binding of regulatory nucleotides to aspartate transcarbamoylase: Nuclear magnetic resonance studies of selectively enriched carbon-13 regulatory subunit
    • Moore, A. C. and Browne, D. T. (1980) Binding of regulatory nucleotides to aspartate transcarbamoylase: nuclear magnetic resonance studies of selectively enriched carbon-13 regulatory subunit Biochemistry 19, 5768-5773
    • (1980) Biochemistry , vol.19 , pp. 5768-5773
    • Moore, A.C.1    Browne, D.T.2
  • 12
    • 0024962397 scopus 로고
    • Lysine-60 in the regulatory chain of Escherichia coli aspartate transcarbamylase is important for the discrimination between CTP and ATP
    • Zhang, Y. and Kantrowitz, E. R. (1989) Lysine-60 in the regulatory chain of Escherichia coli aspartate transcarbamylase is important for the discrimination between CTP and ATP Biochemistry 28, 7313-7318
    • (1989) Biochemistry , vol.28 , pp. 7313-7318
    • Zhang, Y.1    Kantrowitz, E.R.2
  • 13
    • 0023849677 scopus 로고
    • Site-directed mutagenesis of a residue located in the regulatory site of Escherichia coli aspartate transcarbamylase
    • Zhang, Y., Ladjimi, M. M., and Kantrowitz, E. R. (1988) Site-directed mutagenesis of a residue located in the regulatory site of Escherichia coli aspartate transcarbamylase J. Biol. Chem. 263, 1320-1324
    • (1988) J. Biol. Chem. , vol.263 , pp. 1320-1324
    • Zhang, Y.1    Ladjimi, M.M.2    Kantrowitz, E.R.3
  • 14
    • 0025081851 scopus 로고
    • Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate and CTP or ATP at 2.8 Å resolution and neutral pH
    • Gouaux, J. E., Stevens, R. C., and Lipscomb, W. N. (1990) Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate and CTP or ATP at 2.8 Å resolution and neutral pH Biochemistry 29, 7702-7715
    • (1990) Biochemistry , vol.29 , pp. 7702-7715
    • Gouaux, J.E.1    Stevens, R.C.2    Lipscomb, W.N.3
  • 15
    • 0025002987 scopus 로고
    • Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: Crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6 Å resolution
    • Stevens, R. C., Gouaux, J. E., and Lipscomb, W. N. (1990) Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6 Å resolution Biochemistry 29, 7691-7701
    • (1990) Biochemistry , vol.29 , pp. 7691-7701
    • Stevens, R.C.1    Gouaux, J.E.2    Lipscomb, W.N.3
  • 16
    • 21144434991 scopus 로고    scopus 로고
    • Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase
    • Wang, J., Stieglitz, K. A., Cardia, J. P., and Kantrowitz, E. R. (2005) Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase Proc. Natl. Acad. Sci. U.S.A. 102, 8881-8886
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 8881-8886
    • Wang, J.1    Stieglitz, K.A.2    Cardia, J.P.3    Kantrowitz, E.R.4
  • 19
    • 44349141904 scopus 로고    scopus 로고
    • Dissecting enzyme regulation by multiple allosteric effectors: Nucleotide regulation of aspartate transcarbamoylase
    • Rabinowitz, J. D., Hsiao, J. J., Gryncel, K. R., Kantrowitz, E. R., Feng, X. J., Li, G., and Rabitz, H. (2008) Dissecting enzyme regulation by multiple allosteric effectors: nucleotide regulation of aspartate transcarbamoylase Biochemistry 47, 5881-5888
    • (2008) Biochemistry , vol.47 , pp. 5881-5888
    • Rabinowitz, J.D.1    Hsiao, J.J.2    Gryncel, K.R.3    Kantrowitz, E.R.4    Feng, X.J.5    Li, G.6    Rabitz, H.7
  • 21
    • 21144434991 scopus 로고    scopus 로고
    • Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase
    • Wang, J., Stieglitz, K. A., Cardia, J. P., and Kantrowitz, E. R. (2005) Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase Proc. Natl. Acad. Sci. U.S.A. 102, 8881-8886
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 8881-8886
    • Wang, J.1    Stieglitz, K.A.2    Cardia, J.P.3    Kantrowitz, E.R.4
  • 23
    • 0033978887 scopus 로고    scopus 로고
    • Three of the six possible intersubunit stabilizing interactions involving Glu239 are sufficient for restoration of the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylase
    • Sakash, J. B., Chan, R. S., Tsuruta, H., and Kantrowitz, E. R. (2000) Three of the six possible intersubunit stabilizing interactions involving Glu239 are sufficient for restoration of the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylase J. Biol. Chem. 275, 752-758
    • (2000) J. Biol. Chem. , vol.275 , pp. 752-758
    • Sakash, J.B.1    Chan, R.S.2    Tsuruta, H.3    Kantrowitz, E.R.4
  • 24
    • 33745946445 scopus 로고    scopus 로고
    • A genetically encoded fluorescent amino acid
    • Wang, J., Xie, J., and Schultz, P. G. (2006) A genetically encoded fluorescent amino acid J. Am. Chem. Soc. 128, 8738-8739
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 8738-8739
    • Wang, J.1    Xie, J.2    Schultz, P.G.3
  • 25
  • 26
    • 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
  • 27
    • 78651153791 scopus 로고
    • Disc electrophoresis-II. Method and application to human serum proteins
    • Davis, B. J. (1964) Disc electrophoresis-II. Method and application to human serum proteins Ann. N.Y. Acad. Sci. 121, 680-685
    • (1964) Ann. N.Y. Acad. Sci. , vol.121 , pp. 680-685
    • Davis, B.J.1
  • 28
    • 78651163419 scopus 로고
    • Disc electrophoresis-I. Background and theory
    • Ornstein, L. (1964) Disc electrophoresis-I. Background and theory Ann. N.Y. Acad. Sci. 121, 321-349
    • (1964) Ann. N.Y. Acad. Sci. , vol.121 , pp. 321-349
    • Ornstein, L.1
  • 29
    • 0019799867 scopus 로고
    • An improved colorimetric assay for aspartate and ornithine transcarbamylases
    • Pastra-Landis, S. C., Foote, J., and Kantrowitz, E. R. (1981) An improved colorimetric assay for aspartate and ornithine transcarbamylases Anal. Biochem. 118, 358-363
    • (1981) Anal. Biochem. , vol.118 , pp. 358-363
    • Pastra-Landis, S.C.1    Foote, J.2    Kantrowitz, E.R.3
  • 30
    • 0020606654 scopus 로고
    • Analysis of two purified mutants of Escherichia coli aspartate transcarbamylase with single amino acid substitutions
    • Silver, R. S., Daigneault, J. P., Teague, P. D., and Kantrowitz, E. R. (1983) Analysis of two purified mutants of Escherichia coli aspartate transcarbamylase with single amino acid substitutions J. Mol. Biol. 168, 729-745
    • (1983) J. Mol. Biol. , vol.168 , pp. 729-745
    • Silver, R.S.1    Daigneault, J.P.2    Teague, P.D.3    Kantrowitz, E.R.4
  • 31
    • 0017894911 scopus 로고
    • The effect of pH on the cooperative behavior of aspartate transcarbamylase from Escherichia coli
    • Pastra-Landis, S. C., Evans, D. R., and Lipscomb, W. N. (1978) The effect of pH on the cooperative behavior of aspartate transcarbamylase from Escherichia coli J. Biol. Chem. 253, 4624-4630
    • (1978) J. Biol. Chem. , vol.253 , pp. 4624-4630
    • Pastra-Landis, S.C.1    Evans, D.R.2    Lipscomb, W.N.3


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