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Journal Abstract Search

191 related items for PubMed ID: 11467937

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  • 4. Unlike the quaternary structure transition, the tertiary structure change of the 240s loop in allosteric aspartate transcarbamylase requires active site saturation by substrate for completion.
    Fetler L, Vachette P, Hervé G, Ladjimi MM.
    Biochemistry; 1995 Dec 05; 34(48):15654-60. PubMed ID: 7495794
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  • 5. The allosteric activator Mg-ATP modifies the quaternary structure of the R-state of Escherichia coli aspartate transcarbamylase without altering the T<-->R equilibrium.
    Fetler L, Vachette P.
    J Mol Biol; 2001 Jun 08; 309(3):817-32. PubMed ID: 11397099
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  • 8. Site-specific substitutions of the Tyr-165 residue in the catalytic chain of aspartate transcarbamoylase promotes a T-state preference in the holoenzyme.
    Wales ME, Hoover TA, Wild JR.
    J Biol Chem; 1988 May 05; 263(13):6109-14. PubMed ID: 3283120
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  • 12. 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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  • 14. 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 03; 5(11):2276-86. PubMed ID: 8931146
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  • 15. Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase.
    Eisenstein E, Markby DW, Schachman HK.
    Biochemistry; 1990 Apr 17; 29(15):3724-31. PubMed ID: 2187530
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  • 16. Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 A.
    Jin L, Stec B, Lipscomb WN, Kantrowitz ER.
    Proteins; 1999 Dec 01; 37(4):729-42. PubMed ID: 10651286
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  • 18. Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation.
    Endrizzi JA, Beernink PT, Alber T, Schachman HK.
    Proc Natl Acad Sci U S A; 2000 May 09; 97(10):5077-82. PubMed ID: 10805770
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  • 20. Importance of residues Arg-167 and Gln-231 in both the allosteric and catalytic mechanisms of Escherichia coli aspartate transcarbamoylase.
    Stebbins JW, Zhang Y, Kantrowitz ER.
    Biochemistry; 1990 Apr 24; 29(16):3821-7. PubMed ID: 2191720
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