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Journal Abstract Search

269 related items for PubMed ID: 329911

  • 1. A kinetic model of cooperativity in aspartate transcarbamylase.
    Dembo M, Rubinow SI.
    Biophys J; 1977 Jun; 18(3):245-67. PubMed ID: 329911
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  • 2. Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi. Insights into cooperative and allosteric mechanisms.
    Van Boxstael S, Maes D, Cunin R.
    FEBS J; 2005 Jun; 272(11):2670-83. PubMed ID: 15943802
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  • 3. Apparent cooperativity for carbamoylphosphate in Escherichia coli aspartate transcarbamoylase only reflects cooperativity for aspartate.
    England P, Leconte C, Tauc P, Hervé G.
    Eur J Biochem; 1994 Jun 15; 222(3):775-80. PubMed ID: 8026491
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  • 4. 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 15; 3(6):967-74. PubMed ID: 8069226
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  • 6. T-state active site of aspartate transcarbamylase: crystal structure of the carbamyl phosphate and L-alanosine ligated enzyme.
    Huang J, Lipscomb WN.
    Biochemistry; 2006 Jan 17; 45(2):346-52. PubMed ID: 16401065
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  • 7. 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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  • 9. Calorimetric analysis of aspartate transcarbamylase from Escherichia coli. Binding of substrates and substrate analogues to the native enzyme and catalytic subunit.
    Knier BL, Allewell NM.
    Biochemistry; 1978 Mar 07; 17(5):784-90. PubMed ID: 343809
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  • 12. T-state inhibitors of E. coli aspartate transcarbamoylase that prevent the allosteric transition.
    Heng S, Stieglitz KA, Eldo J, Xia J, Cardia JP, Kantrowitz ER.
    Biochemistry; 2006 Aug 22; 45(33):10062-71. PubMed ID: 16906764
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  • 14. 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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  • 17. Kinetics of the quaternary structure change of aspartate transcarbamylase triggered by succinate, a competitive inhibitor.
    Tsuruta H, Vachette P, Sano T, Moody MF, Amemiya Y, Wakabayashi K, Kihara H.
    Biochemistry; 1994 Aug 23; 33(33):10007-12. PubMed ID: 8060968
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  • 18. Three-dimensional structures at 5.5 A resolution and regulatory processes in aspartate transcarbamylase from E. coli.
    Lipscomb WN, Evans DR, Edwards BF, Warren SG, Pastra-Landis S, Wiley DC.
    J Supramol Struct; 1974 Aug 23; 2(2-4):82-98. PubMed ID: 4612257
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  • 19. Nuclear magnetic resonance study of ligand binding to Mn-aspartate transcarbamylase.
    Fan S, Harrison LW, Hammes GG.
    Biochemistry; 1975 May 20; 14(10):2219-24. PubMed ID: 807235
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  • 20. Solvent perturbation of the allosteric regulation of aspartate transcarbamylase.
    LiCata VJ, Allewell NM.
    Biochim Biophys Acta; 1998 May 19; 1384(2):306-14. PubMed ID: 9659392
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