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Journal Abstract Search

133 related items for PubMed ID: 6364987

  • 1. Pyruvate formate-lyase (inactive form) and pyruvate formate-lyase activating enzyme of Escherichia coli: isolation and structural properties.
    Conradt H, Hohmann-Berger M, Hohmann HP, Blaschkowski HP, Knappe J.
    Arch Biochem Biophys; 1984 Jan; 228(1):133-42. PubMed ID: 6364987
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  • 2. Post-translational activation introduces a free radical into pyruvate formate-lyase.
    Knappe J, Neugebauer FA, Blaschkowski HP, Gänzler M.
    Proc Natl Acad Sci U S A; 1984 Mar; 81(5):1332-5. PubMed ID: 6369325
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  • 3. A radical-chemical route to acetyl-CoA: the anaerobically induced pyruvate formate-lyase system of Escherichia coli.
    Knappe J, Sawers G.
    FEMS Microbiol Rev; 1990 Aug; 6(4):383-98. PubMed ID: 2248795
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  • 4. Role of pyruvate and S-adenosylmethioine in activating the pyruvate formate-lyase of Escherichia coli.
    Chase T, Rabinowitz JC.
    J Bacteriol; 1968 Oct; 96(4):1065-78. PubMed ID: 4879554
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  • 5. Catalytic-site mapping of pyruvate formate lyase. Hypophosphite reaction on the acetyl-enzyme intermediate affords carbon-phosphorus bond synthesis (1-hydroxyethylphosphonate).
    Plaga W, Frank R, Knappe J.
    Eur J Biochem; 1988 Dec 15; 178(2):445-50. PubMed ID: 3061816
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  • 6. Molecular properties of pyruvate formate-lyase activating enzyme.
    Wong KK, Murray BW, Lewisch SA, Baxter MK, Ridky TW, Ulissi-DeMario L, Kozarich JW.
    Biochemistry; 1993 Dec 28; 32(51):14102-10. PubMed ID: 8260492
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  • 10. Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme. Molecular properties of the holoenzyme form.
    Külzer R, Pils T, Kappl R, Hüttermann J, Knappe J.
    J Biol Chem; 1998 Feb 27; 273(9):4897-903. PubMed ID: 9478932
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  • 11. Routes of flavodoxin and ferredoxin reduction in Escherichia coli. CoA-acylating pyruvate: flavodoxin and NADPH: flavodoxin oxidoreductases participating in the activation of pyruvate formate-lyase.
    Blaschkowski HP, Neuer G, Ludwig-Festl M, Knappe J.
    Eur J Biochem; 1982 Apr 27; 123(3):563-9. PubMed ID: 7042345
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  • 15. Pyruvate formate-lyase reaction in Escherichia coli. The enzymatic system converting an inactive form of the lyase into the catalytically active enzyme.
    Knappe J, Schacht J, Möckel W, Höpner T, Vetter H, Edenharder R.
    Eur J Biochem; 1969 Dec 27; 11(2):316-27. PubMed ID: 4902610
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