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Volumn 47, Issue 21, 2008, Pages 5881-5888

Dissecting enzyme regulation by multiple allosteric effectors: nucleotide regulation of aspartate transcarbamoylase

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CATALYSIS; NUCLEOTIDES;

EID: 44349141904     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8000566     Document Type: Article
Times cited : (16)

References (36)
  • 1
    • 0024490181 scopus 로고
    • Escherichia coli aspartate transcarbamoylase: Structure, energetics, and catalytic and regulatory mechanisms
    • Allewell, N. M. (1989) Escherichia coli aspartate transcarbamoylase: Structure, energetics, and catalytic and regulatory mechanisms. Annu. Rev. Biophys. Biophys. Chem. 18, 71-92.
    • (1989) Annu. Rev. Biophys. Biophys. Chem , vol.18 , pp. 71-92
    • Allewell, N.M.1
  • 2
    • 0013784860 scopus 로고
    • Distinct subunits for the regulation and catalytic activity of aspartate transcarbamylase
    • Gerhart, J. C., and Schachman, H. K. (1965) Distinct subunits for the regulation and catalytic activity of aspartate transcarbamylase. Biochemistry 4, 1054-1062.
    • (1965) Biochemistry , vol.4 , pp. 1054-1062
    • Gerhart, J.C.1    Schachman, H.K.2
  • 3
    • 0014426672 scopus 로고
    • Crystallographic determination of symmetry of aspartate transcarbamylase
    • Wiley, D. C., and Lipscomb, W. N. (1968) Crystallographic determination of symmetry of aspartate transcarbamylase. Nature 218, 1119-1121.
    • (1968) Nature , vol.218 , pp. 1119-1121
    • Wiley, D.C.1    Lipscomb, W.N.2
  • 4
    • 0014426681 scopus 로고
    • New structural model of E. coli aspartate transcarbamylase and the amino acid sequence of the regulatory polypeptide chain
    • Weber, K. (1968) New structural model of E. coli aspartate transcarbamylase and the amino acid sequence of the regulatory polypeptide chain. Nature 218, 1116-1119.
    • (1968) Nature , vol.218 , pp. 1116-1119
    • Weber, K.1
  • 5
    • 0014669702 scopus 로고
    • Aspartate transcarbamylase. Kinetic studies of the catalytic subunit
    • Porter, R. W., Modebe, M. O., and Stark, G. R. (1969) Aspartate transcarbamylase. Kinetic studies of the catalytic subunit. J. Biol. Chem. 244, 1846-1859.
    • (1969) J. Biol. Chem , vol.244 , pp. 1846-1859
    • Porter, R.W.1    Modebe, M.O.2    Stark, G.R.3
  • 6
    • 0023476420 scopus 로고
    • Kinetic mechanism of native Escherichia coli aspartate transcarbamylase
    • Hsuanyu, Y., and Wedler, F. C. (1987) Kinetic mechanism of native Escherichia coli aspartate transcarbamylase. Arch. Biochem. Biophys. 259, 316-330.
    • (1987) Arch. Biochem. Biophys , vol.259 , pp. 316-330
    • Hsuanyu, Y.1    Wedler, F.C.2
  • 7
    • 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
  • 8
    • 0001738507 scopus 로고
    • Control of pyrimidine biosynthesis in Escherichia coli by a feed-back mechanism
    • Pardee, A. B., and Yates, R. A. (1956) Control of pyrimidine biosynthesis in Escherichia coli by a feed-back mechanism. J. Biol. Chem. 221, 757-770.
    • (1956) J. Biol. Chem , vol.221 , pp. 757-770
    • Pardee, A.B.1    Yates, R.A.2
  • 9
    • 0001425337 scopus 로고
    • The enzymology of control by feedback inhibition
    • Gerhart, J. C., and Pardee, A. B. (1962) The enzymology of control by feedback inhibition. J. Biol. Chem. 237, 891-896.
    • (1962) J. Biol. Chem , vol.237 , pp. 891-896
    • Gerhart, J.C.1    Pardee, A.B.2
  • 10
    • 0017704753 scopus 로고
    • Allosteric regulation of aspartate transcarbamoylase. Effect of active site ligands on the reactivity of sulfhydryl groups of the regulatory subunits
    • Blackburn, M. N., and Schachman, H. K. (1977) Allosteric regulation of aspartate transcarbamoylase. Effect of active site ligands on the reactivity of sulfhydryl groups of the regulatory subunits. Biochemistry 16, 5084-5091.
    • (1977) Biochemistry , vol.16 , pp. 5084-5091
    • Blackburn, M.N.1    Schachman, H.K.2
  • 11
    • 0014253008 scopus 로고
    • Allosteric interactions in aspartate transcarbamylase. II. Evidence for different conformational states of the protein in the presence and absence of specific ligands
    • Gerhart, J. C., and Schachman, H. K. (1968) Allosteric interactions in aspartate transcarbamylase. II. Evidence for different conformational states of the protein in the presence and absence of specific ligands. Biochemistry 7, 538-552.
    • (1968) Biochemistry , vol.7 , pp. 538-552
    • Gerhart, J.C.1    Schachman, H.K.2
  • 12
    • 0017260854 scopus 로고
    • Concerted allosteric transition in hybrids of aspartate transcarbamoylase containing different arrangements of active and inactive sites
    • Gibbons, I., Ritchey, J. M., and Schachman, H. K. (1976) Concerted allosteric transition in hybrids of aspartate transcarbamoylase containing different arrangements of active and inactive sites. Biochemistry 15, 1324-1330.
    • (1976) Biochemistry , vol.15 , pp. 1324-1330
    • Gibbons, I.1    Ritchey, J.M.2    Schachman, H.K.3
  • 13
    • 0021111760 scopus 로고
    • Communication between catalytic and regulatory subunits in Ni(II)- and Co(II)-aspartate transcarbamoylase. Ligand-promoted structural alterations at the intersubunit bonding domains
    • Johnson, R. S., and Schachman, H. K. (1983) Communication between catalytic and regulatory subunits in Ni(II)- and Co(II)-aspartate transcarbamoylase. Ligand-promoted structural alterations at the intersubunit bonding domains. J. Biol. Chem. 258, 3528-3538.
    • (1983) J. Biol. Chem , vol.258 , pp. 3528-3538
    • Johnson, R.S.1    Schachman, H.K.2
  • 14
    • 0023035517 scopus 로고
    • Communication between polypeptide chains in aspartate transcarbamoylase. Conformational changes at the active sites of unliganded chains resulting from ligand binding to other chains
    • Lahue, R. S., and Schachman, H. K. (1986) Communication between polypeptide chains in aspartate transcarbamoylase. Conformational changes at the active sites of unliganded chains resulting from ligand binding to other chains. J. Biol. Chem. 261, 3079-3084.
    • (1986) J. Biol. Chem , vol.261 , pp. 3079-3084
    • Lahue, R.S.1    Schachman, H.K.2
  • 15
    • 0022267976 scopus 로고
    • 19F nuclear magnetic resonance studies of fluorotyrosine-labeled aspartate transcarbamoylase. Properties of the enzyme and its catalytic and regulatory subunits
    • 19F nuclear magnetic resonance studies of fluorotyrosine-labeled aspartate transcarbamoylase. Properties of the enzyme and its catalytic and regulatory subunits. J. Biol. Chem. 260, 11651-11658.
    • (1985) J. Biol. Chem , vol.260 , pp. 11651-11658
    • Wacks, D.B.1    Schachman, H.K.2
  • 16
    • 0024231301 scopus 로고
    • Complex of N-phosphonacetyl-L-aspartate with aspartate carbamoyltransferase. X-ray refinement, analysis of conformational changes and catalytic and allosteric mechanisms
    • Ke, H. M., Lipscomb, W. N., Cho, Y. J., and Honzatko, R. B. (1988) Complex of N-phosphonacetyl-L-aspartate with aspartate carbamoyltransferase. X-ray refinement, analysis of conformational changes and catalytic and allosteric mechanisms. J. Mol. Biol. 204, 725-747.
    • (1988) J. Mol. Biol , vol.204 , pp. 725-747
    • Ke, H.M.1    Lipscomb, W.N.2    Cho, Y.J.3    Honzatko, R.B.4
  • 17
    • 0023819640 scopus 로고
    • Escherichia coli aspartate transcarbamylase: The relation between structure and function
    • Kantrowitz, E. R., and Lipscomb, W. N. (1988) Escherichia coli aspartate transcarbamylase: The relation between structure and function. Science 241, 669-674.
    • (1988) Science , vol.241 , pp. 669-674
    • Kantrowitz, E.R.1    Lipscomb, W.N.2
  • 18
    • 34547604780 scopus 로고    scopus 로고
    • Structural model of the R state of Escherichia coli aspartate transcarbamoylase with substrates bound
    • Wang, J., Eldo, J., and Kantrowitz, E. R. (2007) Structural model of the R state of Escherichia coli aspartate transcarbamoylase with substrates bound. J. Mol. Biol. 371, 1261-1273.
    • (2007) J. Mol. Biol , vol.371 , pp. 1261-1273
    • Wang, J.1    Eldo, J.2    Kantrowitz, E.R.3
  • 19
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J., and Changeux, J.-P. (1965) On the nature of allosteric transitions: A plausible model. J. Mol. Biol. 12, 88-118.
    • (1965) J. Mol. Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 20
    • 0024289426 scopus 로고
    • Can a simple model account for the allosteric transition of aspartate transcarbamoylase?
    • Schachman, H. K. (1988) Can a simple model account for the allosteric transition of aspartate transcarbamoylase? J. Biol. Chem. 263, 18583-18586.
    • (1988) J. Biol. Chem , vol.263 , pp. 18583-18586
    • Schachman, H.K.1
  • 21
    • 33846298432 scopus 로고    scopus 로고
    • Direct observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase
    • Fetler, L., Kantrowitz, E. R., and Vachette, P. (2007) Direct observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase. Proc. Natl. Acad. Sci. U.S.A. 104, 495-500.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 495-500
    • Fetler, L.1    Kantrowitz, E.R.2    Vachette, P.3
  • 22
    • 34547399613 scopus 로고    scopus 로고
    • A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase
    • Velyvis, A., Yang, Y. R., Schachman, H. K., and Kay, L. E. (2007) A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase. Proc. Natl. Acad. Sci. U.S.A. 104, 8815-8820.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 8815-8820
    • Velyvis, A.1    Yang, Y.R.2    Schachman, H.K.3    Kay, L.E.4
  • 23
    • 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
  • 24
    • 0004053611 scopus 로고    scopus 로고
    • 3rd ed, John Wiley and Sons, New York
    • Voet, D., and Voet, J. G. (2004) Biochemistry, 3rd ed., John Wiley and Sons, New York.
    • (2004) Biochemistry
    • Voet, D.1    Voet, J.G.2
  • 25
    • 15244352447 scopus 로고    scopus 로고
    • Modeling allosteric regulation of de novo pyrimidine biosynthesis in Escherichia coli
    • Rodriguez, M., Good, T. A., Wales, M. E., Hua, J. P., and Wild, J. R. (2005) Modeling allosteric regulation of de novo pyrimidine biosynthesis in Escherichia coli. J. Theor. Biol. 234, 299-310.
    • (2005) J. Theor. Biol , vol.234 , pp. 299-310
    • Rodriguez, M.1    Good, T.A.2    Wales, M.E.3    Hua, J.P.4    Wild, J.R.5
  • 27
    • 0035638871 scopus 로고    scopus 로고
    • Efficient implementation of high dimensional model representations
    • Alis, O. F., and Rabitz, H. (2001) Efficient implementation of high dimensional model representations. J. Math. Chem. 29, 127-142.
    • (2001) J. Math. Chem , vol.29 , pp. 127-142
    • Alis, O.F.1    Rabitz, H.2
  • 28
    • 33644918017 scopus 로고    scopus 로고
    • Random sampling-high dimensional model representation (RS-HDMR) and orthogonality of its different order component functions
    • Li, G., Hu, J., Wang, S-W., Georgopoulos, P. G., Schoendorf, J., and Rabitz, H. (2006) Random sampling-high dimensional model representation (RS-HDMR) and orthogonality of its different order component functions. J. Phys. Chem. A 110, 2474-2485.
    • (2006) J. Phys. Chem. A , vol.110 , pp. 2474-2485
    • Li, G.1    Hu, J.2    Wang, S.-W.3    Georgopoulos, P.G.4    Schoendorf, J.5    Rabitz, H.6
  • 29
    • 33748878445 scopus 로고    scopus 로고
    • Kinetic flux profiling of nitrogen assimilation in Escherichia coli
    • Yuan, J., Fowler, W. U., Kimball, E., Lu, W., and Rabinowitz, J. D. (2006) Kinetic flux profiling of nitrogen assimilation in Escherichia coli. Nat. Chem. Biol. 2, 529-530.
    • (2006) Nat. Chem. Biol , vol.2 , pp. 529-530
    • Yuan, J.1    Fowler, W.U.2    Kimball, E.3    Lu, W.4    Rabinowitz, J.D.5
  • 30
    • 0022382162 scopus 로고
    • Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway
    • Nowlan, S. F., and Kantrowitz, E. R. (1985) Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway. J. Biol. Chem. 260, 14712-14716.
    • (1985) J. Biol. Chem , vol.260 , pp. 14712-14716
    • Nowlan, S.F.1    Kantrowitz, E.R.2
  • 31
    • 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
  • 33
    • 38749142232 scopus 로고    scopus 로고
    • Characterization of nucleotide pools as a function of physiological state in Escherichia coli
    • Buckstein, M. H., He, J., and Rubin, H. (2008) Characterization of nucleotide pools as a function of physiological state in Escherichia coli. J. Bacteriol. 190, 718-726.
    • (2008) J. Bacteriol , vol.190 , pp. 718-726
    • Buckstein, M.H.1    He, J.2    Rubin, H.3
  • 34
    • 34548023950 scopus 로고    scopus 로고
    • Acidic acetonitrile for cellular metabolome extraction from Escherichia coli
    • Rabinowitz, J. D., and Kimball, E. (2007) Acidic acetonitrile for cellular metabolome extraction from Escherichia coli. Anal. Chem. 79, 6167-6173.
    • (2007) Anal. Chem , vol.79 , pp. 6167-6173
    • Rabinowitz, J.D.1    Kimball, E.2
  • 35
    • 0020443521 scopus 로고
    • Complete analysis of cellular nucleotides by two-dimensional thin layer chromatography
    • Bochner, B. R., and Ames, B. N. (1982) Complete analysis of cellular nucleotides by two-dimensional thin layer chromatography. J. Biol. Chem. 257, 9759-9769.
    • (1982) J. Biol. Chem , vol.257 , pp. 9759-9769
    • Bochner, B.R.1    Ames, B.N.2
  • 36
    • 0024501782 scopus 로고
    • Three residues involved in binding and catalysis in the carbamyl phosphate binding site of Escherichia coli aspartate transcarbamylase
    • Stebbins, J. W., Xu, W., and Kantrowitz, E. R. (1989) Three residues involved in binding and catalysis in the carbamyl phosphate binding site of Escherichia coli aspartate transcarbamylase. Biochemistry 28, 2592-2600.
    • (1989) Biochemistry , vol.28 , pp. 2592-2600
    • Stebbins, J.W.1    Xu, W.2    Kantrowitz, E.R.3


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