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282 related items for PubMed ID: 8476846

  • 1. Site-directed alterations to the geometry of the aspartate transcarbamoylase zinc domain: selective alteration to regulation by heterotropic ligands, isoelectric point, and stability in urea.
    Strang CJ, Wales ME, Brown DM, Wild JR.
    Biochemistry; 1993 Apr 27; 32(16):4156-67. PubMed ID: 8476846
    [Abstract] [Full Text] [Related]

  • 2. Threonine 82 in the regulatory chain is important for nucleotide affinity and for the allosteric stabilization of Escherichia coli aspartate transcarbamoylase.
    Williams MK, Kantrowitz ER.
    Biochim Biophys Acta; 1998 Dec 08; 1429(1):249-58. PubMed ID: 9920401
    [Abstract] [Full Text] [Related]

  • 3. Role of allosteric: zinc interdomain region of the regulatory subunit in the allosteric regulation of aspartate transcarbamoylase from Escherichia coli.
    Rastogi VK, Swanson R, Hartberg YM, Wales ME, Wild JR.
    Arch Biochem Biophys; 1998 Jun 15; 354(2):215-24. PubMed ID: 9637729
    [Abstract] [Full Text] [Related]

  • 4. The allosteric activator ATP induces a substrate-dependent alteration of the quaternary structure of a mutant aspartate transcarbamoylase impaired in active site closure.
    Baker DP, Fetler L, Vachette P, Kantrowitz ER.
    Protein Sci; 1996 Nov 15; 5(11):2276-86. PubMed ID: 8931146
    [Abstract] [Full Text] [Related]

  • 5. The N-terminus of the regulatory chain of Escherichia coli aspartate transcarbamoylase is important for both nucleotide binding and heterotropic effects.
    Sakash JB, Kantrowitz ER.
    Biochemistry; 1998 Jan 06; 37(1):281-8. PubMed ID: 9425049
    [Abstract] [Full Text] [Related]

  • 6. Probing the regulatory site of Escherichia coli aspartate transcarbamoylase by site-specific mutagenesis.
    Zhang Y, Kantrowitz ER.
    Biochemistry; 1992 Jan 28; 31(3):792-8. PubMed ID: 1731936
    [Abstract] [Full Text] [Related]

  • 7. Divergent allosteric patterns verify the regulatory paradigm for aspartate transcarbamylase.
    Wales ME, Madison LL, Glaser SS, Wild JR.
    J Mol Biol; 1999 Dec 17; 294(5):1387-400. PubMed ID: 10600393
    [Abstract] [Full Text] [Related]

  • 8. Three of the six possible intersubunit stabilizing interactions involving Glu-239 are sufficient for restoration of the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylase.
    Sakash JB, Chan RS, Tsuruta H, Kantrowitz ER.
    J Biol Chem; 2000 Jan 14; 275(2):752-8. PubMed ID: 10625604
    [Abstract] [Full Text] [Related]

  • 9. Discrimination between nucleotide effector responses of aspartate transcarbamoylase due to a single site substitution in the allosteric binding site.
    Corder TS, Wild JR.
    J Biol Chem; 1989 May 05; 264(13):7425-30. PubMed ID: 2651439
    [Abstract] [Full Text] [Related]

  • 10. Heterotropic interactions in aspartate transcarbamoylase: turning allosteric ATP activation into inhibition as a consequence of a single tyrosine to phenylalanine mutation.
    Van Vliet F, Xi XG, De Staercke C, de Wannemaeker B, Jacobs A, Cherfils J, Ladjimi MM, Hervé G, Cunin R.
    Proc Natl Acad Sci U S A; 1991 Oct 15; 88(20):9180-3. PubMed ID: 1924381
    [Abstract] [Full Text] [Related]

  • 11. The use of alanine scanning mutagenesis to determine the role of the N-terminus of the regulatory chain in the heterotropic mechanism of Escherichia coli aspartate transcarbamoylase.
    Dembowski NJ, Kantrowitz ER.
    Protein Eng; 1994 May 15; 7(5):673-9. PubMed ID: 8073037
    [Abstract] [Full Text] [Related]

  • 12. Conversion of the allosteric regulatory patterns of aspartate transcarbamoylase by exchange of a single beta-strand between diverged regulatory chains.
    Liu L, Wales ME, Wild JR.
    Biochemistry; 1997 Mar 18; 36(11):3126-32. PubMed ID: 9115988
    [Abstract] [Full Text] [Related]

  • 13. Weakening of the interface between adjacent catalytic chains promotes domain closure in Escherichia coli aspartate transcarbamoylase.
    Baker DP, Fetler L, Keiser RT, Vachette P, Kantrowitz ER.
    Protein Sci; 1995 Feb 18; 4(2):258-67. PubMed ID: 7757014
    [Abstract] [Full Text] [Related]

  • 14. 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, Kantrowitz ER.
    J Biol Chem; 1991 Nov 25; 266(33):22154-8. PubMed ID: 1939236
    [Abstract] [Full Text] [Related]

  • 15. Lysine-60 in the regulatory chain of Escherichia coli aspartate transcarbamoylase is important for the discrimination between CTP and ATP.
    Zhang Y, Kantrowitz ER.
    Biochemistry; 1989 Sep 05; 28(18):7313-8. PubMed ID: 2510822
    [Abstract] [Full Text] [Related]

  • 16. Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains.
    Eisenstein E, Markby DW, Schachman HK.
    Proc Natl Acad Sci U S A; 1989 May 05; 86(9):3094-8. PubMed ID: 2566165
    [Abstract] [Full Text] [Related]

  • 17. A single mutation in the regulatory chain of Escherichia coli aspartate transcarbamoylase results in an extreme T-state structure.
    Williams MK, Stec B, Kantrowitz ER.
    J Mol Biol; 1998 Aug 07; 281(1):121-34. PubMed ID: 9680480
    [Abstract] [Full Text] [Related]

  • 18. Importance of a conserved residue, aspartate-162, for the function of Escherichia coli aspartate transcarbamoylase.
    Newton CJ, Stevens RC, Kantrowitz ER.
    Biochemistry; 1992 Mar 24; 31(11):3026-32. PubMed ID: 1550826
    [Abstract] [Full Text] [Related]

  • 19. Amino acid substitutions which stabilize aspartate transcarbamoylase in the R state disrupt both homotropic and heterotropic effects.
    Newell JO, Schachman HK.
    Biophys Chem; 1990 Aug 31; 37(1-3):183-96. PubMed ID: 2285780
    [Abstract] [Full Text] [Related]

  • 20. Different amino acid substitutions at the same position in the nucleotide-binding site of aspartate transcarbamoylase have diverse effects on the allosteric properties of the enzyme.
    Wente SR, Schachman HK.
    J Biol Chem; 1991 Nov 05; 266(31):20833-9. PubMed ID: 1939134
    [Abstract] [Full Text] [Related]

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