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Journal Abstract Search

142 related items for PubMed ID: 328500

  • 1. 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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  • 2. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Carboxymethylation of the enzyme: threonine binding and inhibition are functionally dissociable.
    Fontan E, Truffa-Bachi P.
    J Biol Chem; 1978 Apr 25; 253(8):2754-7. PubMed ID: 344322
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  • 6. 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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  • 7. Reversible dissociation of aspartokinase I/homoserine dehydrogenase I from Escherichia coli K 12. The active species is the tetramer.
    Veron M, Guillou Y, Fazel A, Cohen GN.
    Eur J Biochem; 1985 Sep 16; 151(3):521-4. PubMed ID: 3896789
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  • 8. 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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  • 12. 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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  • 13. The interaction between Escherichia coli aspartokinase-homoserine dehydrogenase and 3-acetylpyridine-adenine dinucleotide phosphate (reduced), an analog of NADPH.
    Müller K, Garel JR.
    J Biol Chem; 1984 Feb 25; 259(4):2252-6. PubMed ID: 6365907
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  • 15. 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
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  • 17. E. coli aspartokinase II-homoserine dehydrogenase II polypeptide chain has a triglobular structure.
    Belfaiza J, Fazel A, Müller K, Cohen GN.
    Biochem Biophys Res Commun; 1984 Aug 30; 123(1):16-20. PubMed ID: 6383377
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  • 19. Structure, function, and possible origin of a bifunctional allosteric enzyme, Escherichia coli aspartokinase I-homoserine dehydrogenase I.
    Truffa-Bachi P, Veron M, Cohen GN.
    CRC Crit Rev Biochem; 1974 Aug 30; 2(3):379-415. PubMed ID: 4155358
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