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255 related items for PubMed ID: 192265

  • 1. Interaction of substrates and inhibitors with the homoserine dehydrogenase of kinase-inactivated aspartokinase I.
    Wright JK, Takahashi M.
    Biochemistry; 1977 Apr 19; 16(8):1541-8. PubMed ID: 192265
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  • 2. Cobalt(III) affinity-labeled aspartokinase. Formation of substrate and inhibitor adducts.
    Wright JK, Feldman J, Takahashi M.
    Biochemistry; 1976 Aug 24; 15(17):3704-10. PubMed ID: 182215
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  • 3. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K-12. Incubation of the enzyme in alkaline conditions: dissociation and disulfide-bridge formation.
    Jacques Y, Truffa-Bachi P.
    Eur J Biochem; 1976 Mar 01; 62(3):485-90. PubMed ID: 4302
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  • 4. Cobalt(III) labeled aspartokinase-homoserine dehydrogenase of Escherichia coli.
    Ryzewski C, Takahashi MT.
    Biochemistry; 1975 Oct 07; 14(20):4482-6. PubMed ID: 1100105
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  • 5. Aspartokinase I-homoserine dehydrogenase I of Escherichia coli K12 (lambda). Activation by monovalent cations and an analysis of the effect of the adenosine triphosphate-magnesium ion complex on this activation process.
    Ogilvie JW, Vickers LP, Clark RB, Jones MM.
    J Biol Chem; 1975 Feb 25; 250(4):1242-50. PubMed ID: 163250
    [Abstract] [Full Text] [Related]

  • 6. Fluorescence energy transfer between heterologous active sites of affinity-labeled aspartokinase of Escherichia coli.
    Wright K, Takahashi M.
    Biochemistry; 1977 Apr 19; 16(8):1548-54. PubMed ID: 192266
    [Abstract] [Full Text] [Related]

  • 7. Fluorescence studies of threonine-promoted conformational transitions in aspartokinase I using the substrate analogue 2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate.
    Broglie KE, Takahashi M.
    J Biol Chem; 1983 Nov 10; 258(21):12940-6. PubMed ID: 6313682
    [Abstract] [Full Text] [Related]

  • 8. A hybrid proteolytic fragment of Escherichia coli aspartokinase I-homoserine dehydrogenase I. Structure, inhibition pattern, dissociation properties, and generation of two homodimers.
    Fazel A, Guillou Y, Cohen GN.
    J Biol Chem; 1983 Nov 25; 258(22):13570-4. PubMed ID: 6315703
    [Abstract] [Full Text] [Related]

  • 9. Proteolysis of the bifunctional methionine-repressible aspartokinase II-homoserine dehydrogenase II of Escherichia coli K12. Production of an active homoserine dehydrogenase fragment.
    Dautry-Varsat A, Cohen GN.
    J Biol Chem; 1977 Nov 10; 252(21):7685-9. PubMed ID: 334767
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  • 18. Evolution of biosynthetic pathways: immunological approach.
    Truffa-Bachi P, Guiso N, Cohen GN, Theze J, Burr B.
    Proc Natl Acad Sci U S A; 1975 Apr 10; 72(4):1268-71. PubMed ID: 48255
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  • 19. Threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Kinetic and spectroscopic effects upon binding of serine and threonine.
    Costrejean JM, Truffa-Bachi P.
    J Biol Chem; 1977 Aug 10; 252(15):5332-6. PubMed ID: 328500
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  • 20. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Specific inactivation of the homoserine dehydrogenase activity by the affinity label, 2-amino-4-oxo-5-chloropentanoic acid.
    Hirth CG, Véron M, Villar-Palasi C, Hurion N, Cohen GN.
    Eur J Biochem; 1975 Jan 02; 50(2):425-30. PubMed ID: 236185
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