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Journal Abstract Search

134 related items for PubMed ID: 334767

  • 21. 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]

  • 22. Immunological cross reactivity of four enzymes involved in the biosynthetic pathway of lysine, methionine and threonine in Escherichia coli K12.
    Truffa-Bachi P.
    Acta Microbiol Acad Sci Hung; 1976 Feb 25; 23(2):129-35. PubMed ID: 61712
    [Abstract] [Full Text] [Related]

  • 23. Proceedings: Organization of Escherichia coli aspartokinase I-Homoserine dehydrogenase I, an allosteric enzyme. -- Its possible origin by gene fusion and its evolutionary relationship with enzymes of the same biochemical pathway.
    Cohen GN.
    Hoppe Seylers Z Physiol Chem; 1975 Mar 25; 356(3):224-5. PubMed ID: 1102410
    [No Abstract] [Full Text] [Related]

  • 24. Regulation of aspartokinase and homoserine dehydrogenase in acetic acid bacteria.
    O'Sullivan J, Ettlinger L.
    Antonie Van Leeuwenhoek; 1975 Mar 25; 41(1):113-8. PubMed ID: 168808
    [Abstract] [Full Text] [Related]

  • 25. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Distribution and accessibility to antibodies of some epitopes of the bifunctional enzyme.
    Costrejean JM, Guiso N, Cowie DB, Cohen GN, Truffa-Bachi P.
    Eur J Biochem; 1975 Jan 02; 50(2):431-5. PubMed ID: 47808
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  • 26. 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 Jan 02; 2(3):379-415. PubMed ID: 4155358
    [No Abstract] [Full Text] [Related]

  • 27. The primary structure of Escherichia coli K12 aspartokinase I-homoserine dehydrogenase I. Distribution of the methioninyl residues and of the cysteinyl and tryptophanyl tryptic peptides.
    Sibilli L, Cossart P, Chalvignac MA, Briley PA, Costrejean JM, Le Bras G, Cohen GN.
    Biochimie; 1977 Jan 02; 59(11-12):943-6. PubMed ID: 343821
    [No Abstract] [Full Text] [Related]

  • 28. Aspartate kinases I, II, and III from Escherichia coli.
    Cohen GN.
    Methods Enzymol; 1985 Jan 02; 113():596-9. PubMed ID: 3003511
    [No Abstract] [Full Text] [Related]

  • 29. Threonine inhibition of the aspartokinase--homoserine dehydrogenase I of Escherichia coli. Stopped-flow kinetics and the cooperativity of inhibition of the homoserine dehydrogenase activity.
    Bearer CF, Neet KE.
    Biochemistry; 1978 Aug 22; 17(17):3517-22. PubMed ID: 28751
    [No Abstract] [Full Text] [Related]

  • 30. The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. Carboxymethylation of a unique cysteine induces a conformational change of the enzyme.
    Fontan E, Truffa-Bachi P.
    J Biol Chem; 1978 Apr 25; 253(8):2758-62. PubMed ID: 344323
    [No Abstract] [Full Text] [Related]

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  • 32. Nucleotide sequence of the metL gene of Escherichia coli. Its product, the bifunctional aspartokinase ii-homoserine dehydrogenase II, and the bifunctional product of the thrA gene, aspartokinase I-homoserine dehydrogenase I, derive from a common ancestor.
    Zakin MM, Duchange N, Ferrara P, Cohen GN.
    J Biol Chem; 1983 Mar 10; 258(5):3028-31. PubMed ID: 6298218
    [No Abstract] [Full Text] [Related]

  • 33. Stepwise inactivation of Escherichia coli aspartokinase-homoserine dehydrogenase I.
    Müller K, Garel JR.
    Biochemistry; 1984 Feb 14; 23(4):651-4. PubMed ID: 6370302
    [Abstract] [Full Text] [Related]

  • 34. Activities and regulation of the enzymes involved in the first and the third steps of the aspartate biosynthetic pathway in Enterococcus faecium.
    Kalcheva EO, Shanskaya VO, Maliuta SS.
    Arch Microbiol; 1994 Feb 14; 161(4):359-62. PubMed ID: 8002714
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  • 36. The kinetic mechanisms of the bifunctional enzyme aspartokinase-homoserine dehydrogenase I from Escherichia coli.
    Angeles TS, Viola RE.
    Arch Biochem Biophys; 1990 Nov 15; 283(1):96-101. PubMed ID: 2241177
    [Abstract] [Full Text] [Related]

  • 37. Folding of aspartokinase-homoserine dehydrogenase I is dominated by tertiary interactions.
    Müller K, Garel JR.
    Biochemistry; 1984 Feb 14; 23(4):655-60. PubMed ID: 6370303
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  • 40. Aspartokinase-homoserine dehydrogenase I from Escherichia coli: pH and chemical modification studies of the kinase activity.
    Angeles TS, Smanik PA, Borders CL, Viola RE.
    Biochemistry; 1989 Oct 31; 28(22):8771-7. PubMed ID: 2557908
    [Abstract] [Full Text] [Related]

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