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197 related items for PubMed ID: 2252907

  • 1. The catalytic site of Escherichia coli aspartate transcarbamylase: interaction between histidine 134 and the carbonyl group of the substrate carbamyl phosphate.
    Xi XG, Van Vliet F, Ladjimi MM, Cunin R, Hervé G.
    Biochemistry; 1990 Sep 11; 29(36):8491-8. PubMed ID: 2252907
    [Abstract] [Full Text] [Related]

  • 2. Three residues involved in binding and catalysis in the carbamyl phosphate binding site of Escherichia coli aspartate transcarbamylase.
    Stebbins JW, Xu W, Kantrowitz ER.
    Biochemistry; 1989 Mar 21; 28(6):2592-600. PubMed ID: 2659074
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  • 6. 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
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  • 8. Function of threonine-55 in the carbamoyl phosphate binding site of Escherichia coli aspartate transcarbamoylase.
    Xu W, Kantrowitz ER.
    Biochemistry; 1989 Dec 26; 28(26):9937-43. PubMed ID: 2515892
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  • 9. The catalytic mechanism of Escherichia coli aspartate carbamoyltransferase: a molecular modelling study.
    Gouaux JE, Krause KL, Lipscomb WN.
    Biochem Biophys Res Commun; 1987 Feb 13; 142(3):893-7. PubMed ID: 3548720
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  • 10. Ionization of amino acid residues involved in the catalytic mechanism of aspartate transcarbamoylase.
    Turnbull JL, Waldrop GL, Schachman HK.
    Biochemistry; 1992 Jul 21; 31(28):6562-9. PubMed ID: 1633167
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  • 11. The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativity.
    Macol C, Dutta M, Stec B, Tsuruta H, Kantrowitz ER.
    Protein Sci; 1999 Jun 21; 8(6):1305-13. PubMed ID: 10386880
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  • 12. Kinetic mechanism of catalytic subunits (c3) of E. coli aspartate transcarbamylase at pH 7.0.
    Hsuanyu Y, Wedler FC.
    Biochim Biophys Acta; 1988 Dec 02; 957(3):455-8. PubMed ID: 3058211
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  • 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 02; 4(2):258-67. PubMed ID: 7757014
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  • 14. Evidence from 13C NMR for protonation of carbamyl-P and N-(phosphonacetyl)-L-aspartate in the active site of aspartate transcarbamylase.
    Roberts MF, Opella SJ, Schaffer MH, Phillips HM, Stark GR.
    J Biol Chem; 1976 Oct 10; 251(19):5976-85. PubMed ID: 9410
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  • 15. A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transition.
    Stieglitz KA, Pastra-Landis SC, Xia J, Tsuruta H, Kantrowitz ER.
    J Mol Biol; 2005 Jun 03; 349(2):413-23. PubMed ID: 15890205
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  • 16. Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanine.
    Waldrop GL, Turnbull JL, Parmentier LE, O'Leary MH, Cleland WW, Schachman HK.
    Biochemistry; 1992 Jul 21; 31(28):6585-91. PubMed ID: 1633170
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  • 17. The contribution of threonine 55 to catalysis in aspartate transcarbamoylase.
    Waldrop GL, Turnbull JL, Parmentier LE, Lee S, O'Leary MH, Cleland WW, Schachman HK.
    Biochemistry; 1992 Jul 21; 31(28):6592-7. PubMed ID: 1633171
    [Abstract] [Full Text] [Related]

  • 18. Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: thermostability and 1.8A resolution crystal structure of the catalytic subunit complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate.
    Van Boxstael S, Cunin R, Khan S, Maes D.
    J Mol Biol; 2003 Feb 07; 326(1):203-16. PubMed ID: 12547202
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  • 19. Structural consequences of the replacement of Glu239 by Gln in the catalytic chain of Escherichia coli aspartate transcarbamylase.
    Tauc P, Vachette P, Middleton SA, Kantrowitz ER.
    J Mol Biol; 1990 Jul 05; 214(1):327-35. PubMed ID: 1973463
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  • 20. A loop involving catalytic chain residues 230-245 is essential for the stabilization of both allosteric forms of Escherichia coli aspartate transcarbamylase.
    Middleton SA, Stebbins JW, Kantrowitz ER.
    Biochemistry; 1989 Feb 21; 28(4):1617-26. PubMed ID: 2655696
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