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Journal Abstract Search

249 related items for PubMed ID: 3058211

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  • 2. A 70-amino acid zinc-binding polypeptide fragment from the regulatory chain of aspartate transcarbamoylase causes marked changes in the kinetic mechanism of the catalytic trimer.
    Zhou BB, Waldrop GL, Lum L, Schachman HK.
    Protein Sci; 1994 Jun; 3(6):967-74. PubMed ID: 8069226
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  • 4. Site-specific mutation of Tyr240----Phe in the catalytic chain of Escherichia coli aspartate transcarbamylase. Consequences for kinetic mechanism.
    Hsuanyu Y, Wedler FC, Kantrowitz ER, Middleton SA.
    J Biol Chem; 1989 Oct 15; 264(29):17259-65. PubMed ID: 2677001
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  • 5. Changes in the hydrogen exchange kinetics of Escherichia coli aspartate transcarbamylase produced by effector binding and subunit association.
    Lennick M, Allewell NM.
    Proc Natl Acad Sci U S A; 1981 Nov 15; 78(11):6759-63. PubMed ID: 7031660
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  • 7. Kinetic mechanism of native Escherichia coli aspartate transcarbamylase.
    Hsuanyu Y, Wedler FC.
    Arch Biochem Biophys; 1987 Dec 15; 259(2):316-30. PubMed ID: 3322196
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  • 10. The effect of pH on the cooperative behavior of aspartate transcarbamylase from Escherichia coli.
    Pastra-Landis SC, Evans DR, Lipscomb WN.
    J Biol Chem; 1978 Jul 10; 253(13):4624-30. PubMed ID: 26686
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  • 12. 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
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  • 13. 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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  • 15. L-aspartate association contributes to rate limitation and induction of the T-->R transition in Escherichia coli aspartate transcarbamoylase. Equilibrium exchanges and kinetic isotope effects with a Vmax-enhanced mutant, Asp-236-->Ala.
    Wedler FC, Ley BW, Lee BH, O'Leary MH, Kantrowitz ER.
    J Biol Chem; 1995 Apr 28; 270(17):9725-33. PubMed ID: 7730350
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  • 19. Bohr effect in Escherichia coli aspartate transcarbamylase. Linkages between substrate binding, proton binding, and conformational transitions.
    Allwell NM, Hofmann GE, Zaug A, Lennick M.
    Biochemistry; 1979 Jul 10; 18(14):3008-15. PubMed ID: 37893
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  • 20. 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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