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PUBMED FOR HANDHELDS

Journal Abstract Search


149 related items for PubMed ID: 4604737

  • 1. Mechanism of the reaction catalyzed by the catalytic subunit of aspartate transcarbamylase. Kinetic studies with acetyl phosphate as substrate.
    Heyde E, Morrison JF.
    Biochemistry; 1973 Nov 06; 12(23):4727-32. PubMed ID: 4604737
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  • 6. Aspartate transcarbamylase from Streptococcus faecalis. Steady-state kinetic analysis.
    Chang TY, Jones ME.
    Biochemistry; 1974 Feb 12; 13(4):638-45. PubMed ID: 4359463
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  • 7. Interaction of aspartate transcarbamylase with 5-bromocytidine 5'-tri-, di-, and monophosphates.
    Tondre C, Hammes GG.
    Biochemistry; 1974 Jul 16; 13(15):3131-6. PubMed ID: 4601429
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  • 9. Carbamyl phosphate binding to aspartate transcarbamylase. Partial saturation and its alteration by succinate.
    Rosenbusch JP, Griffin JH.
    J Biol Chem; 1973 Jul 25; 248(14):5063-6. PubMed ID: 4577764
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  • 10. Aspartate transcarbamylase of Escherichia coli. Mechanisms of inhibition and activation by dicarboxylic acids and other anions.
    Jacobson GR, Stark GR.
    J Biol Chem; 1975 Sep 10; 250(17):6852-60. PubMed ID: 1099096
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  • 11. Modification of three active site lysine residues in the catalytic subunit of aspartate transcarbamylase by D- and L-bromosuccinate.
    Lauritzen AM, Lipscomb WN.
    J Biol Chem; 1982 Feb 10; 257(3):1312-9. PubMed ID: 6799505
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  • 13. Conformational studies on the nitrated catalytic subunit of aspartate transcarbamylase.
    Kirschner MW, Schachman HK.
    Biochemistry; 1973 Jul 31; 12(16):2987-97. PubMed ID: 4730495
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  • 15. Relaxation spectra of aspartate transcarbamylase. Interaction of the catalytic subunit with carbamyl phosphate, succinate, and L-malate.
    Hammes GG, Porter RW, Stark GR.
    Biochemistry; 1971 Mar 16; 10(6):1046-50. PubMed ID: 4927803
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  • 17. L-alanosine: a noncooperative substrate for Escherichia coli aspartate transcarbamylase.
    Baillon J, Tauc P, Hervé G.
    Biochemistry; 1985 Dec 03; 24(25):7182-7. PubMed ID: 3910096
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  • 19. The binding of N-(phosphonacetyl)-L-aspartate to aspartate carbamoyltransferase of Escherichia coli.
    Volź KW, Krause KL, Lipscomb WN.
    Biochem Biophys Res Commun; 1986 Apr 29; 136(2):822-6. PubMed ID: 3518720
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  • 20. 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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