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Journal Abstract Search

157 related items for PubMed ID: 2285780

  • 21. In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: implications for protein folding and assembly.
    Zhang P, Schachman HK.
    Protein Sci; 1996 Jul; 5(7):1290-300. PubMed ID: 8819162
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  • 23. 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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  • 24. A fluorescent probe-labeled Escherichia coli aspartate transcarbamoylase that monitors the allosteric conformational state.
    West JM, Tsuruta H, Kantrowitz ER.
    J Biol Chem; 2004 Jan 09; 279(2):945-51. PubMed ID: 14581486
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  • 25. The contribution of individual interchain interactions to the stabilization of the T and R states of Escherichia coli aspartate transcarbamoylase.
    Sakash JB, Kantrowitz ER.
    J Biol Chem; 2000 Sep 15; 275(37):28701-7. PubMed ID: 10875936
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  • 28. In vivo formation of active aspartate transcarbamoylase from complementing fragments of the catalytic polypeptide chains.
    Yang YR, Schachman HK.
    Protein Sci; 1993 Jun 15; 2(6):1013-23. PubMed ID: 8318886
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  • 30. Homotropic effects in aspartate transcarbamoylase. What happens when the enzyme binds a single molecule of the bisubstrate analog N-phosphonacetyl-L-aspartate?
    Foote J, Schachman HK.
    J Mol Biol; 1985 Nov 05; 186(1):175-84. PubMed ID: 3908690
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  • 31. Effects of replacement of active site residue glutamine 231 on activity and allosteric properties of aspartate transcarbamoylase.
    Peterson CB, Burman DL, Schachman HK.
    Biochemistry; 1992 Sep 15; 31(36):8508-15. PubMed ID: 1390636
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  • 34. Domain closure in the catalytic chains of Escherichia coli aspartate transcarbamoylase influences the kinetic mechanism.
    Lee BH, Ley BW, Kantrowitz ER, O'Leary MH, Wedler FC.
    J Biol Chem; 1995 Jun 30; 270(26):15620-7. PubMed ID: 7797560
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  • 35. A 70-amino acid zinc-binding polypeptide from the regulatory chain of aspartate transcarbamoylase forms a stable complex with the catalytic subunit leading to markedly altered enzyme activity.
    Markby DW, Zhou BB, Schachman HK.
    Proc Natl Acad Sci U S A; 1991 Dec 01; 88(23):10568-72. PubMed ID: 1961722
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  • 37. 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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  • 38. Importance of domain closure for homotropic cooperativity in Escherichia coli aspartate transcarbamylase.
    Newton CJ, Kantrowitz ER.
    Biochemistry; 1990 Feb 13; 29(6):1444-51. PubMed ID: 2185840
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  • 39. 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
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  • 40. 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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