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Journal Abstract Search


345 related items for PubMed ID: 10651286

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  • 4. Complex of N-phosphonacetyl-L-aspartate with aspartate carbamoyltransferase. X-ray refinement, analysis of conformational changes and catalytic and allosteric mechanisms.
    Ke HM, Lipscomb WN, Cho YJ, Honzatko RB.
    J Mol Biol; 1988 Dec 05; 204(3):725-47. PubMed ID: 3066911
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  • 5. 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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  • 9. Peptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase.
    Zhou BB, Schachman HK.
    Protein Sci; 1993 Jan 09; 2(1):103-12. PubMed ID: 8443583
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  • 10. Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, NMR, and X-ray crystallographic study.
    Stebbins JW, Robertson DE, Roberts MF, Stevens RC, Lipscomb WN, Kantrowitz ER.
    Protein Sci; 1992 Nov 09; 1(11):1435-46. PubMed ID: 1303763
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  • 13. Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase.
    Fetler L, Tauc P, Baker DP, Macol CP, Kantrowitz ER, Vachette P.
    Protein Sci; 2002 May 09; 11(5):1074-81. PubMed ID: 11967364
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  • 17. Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes.
    Endrizzi JA, Beernink PT.
    Protein Sci; 2017 Nov 09; 26(11):2221-2228. PubMed ID: 28833948
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  • 20. 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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