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189 related items for PubMed ID: 4015669

  • 1. The effect of thiamine pyrophosphate modification on its coenzyme function in a transketolase-catalyzed reaction.
    Usmanov RA, Neef H, Pustynnikov MG, Schellenberger A, Kochetov GA.
    Biochem Int; 1985 Mar; 10(3):479-86. PubMed ID: 4015669
    [Abstract] [Full Text] [Related]

  • 2. Interaction of dihydroxyethylthiamine pyrophosphate with transketolase.
    Usmanov RA, Sidorova NN, Kochetov GA.
    Biochem Mol Biol Int; 1996 Feb; 38(2):307-14. PubMed ID: 8850526
    [Abstract] [Full Text] [Related]

  • 3. [Function of the arginine residue in the active center of baker's yeast transketolase].
    Usmanov RA, Kochetov GA.
    Biokhimiia; 1983 May; 48(5):772-81. PubMed ID: 6347264
    [Abstract] [Full Text] [Related]

  • 4. Interaction of baker's yeast transketolase modified by 2,3-butanedione with anionic and nonanionic substrates.
    Usmanov RA, Kochetov GA.
    Biochem Int; 1983 May; 6(5):673-83. PubMed ID: 6385978
    [Abstract] [Full Text] [Related]

  • 5. Kinetic investigation of cooperativity in coenzyme binding by transketolase active sites.
    Kovina MV, Selivanov VA, Kochevova NV, Kochetov GA.
    Biochemistry (Mosc); 1998 Aug; 63(8):988-95. PubMed ID: 9767190
    [Abstract] [Full Text] [Related]

  • 6. [Kinetics of dissociation and reactivation of rat liver holotransketolase].
    Kubyshin VL, Tomasheva EV, Kulesh IV, Gorbach ZV.
    Ukr Biokhim Zh (1999); 2012 Aug; 84(5):48-54. PubMed ID: 23342634
    [Abstract] [Full Text] [Related]

  • 7. Identification of catalytically important residues in yeast transketolase.
    Wikner C, Nilsson U, Meshalkina L, Udekwu C, Lindqvist Y, Schneider G.
    Biochemistry; 1997 Dec 16; 36(50):15643-9. PubMed ID: 9398292
    [Abstract] [Full Text] [Related]

  • 8. [Metabolism of transketolase coenzyme in the rat liver].
    Gorbach ZV, Kubyshin VL, Maglysh SS, Zabrodskaia SV.
    Biokhimiia; 1986 Jul 16; 51(7):1093-9. PubMed ID: 3730445
    [Abstract] [Full Text] [Related]

  • 9. 2-Acetylthiamin pyrophosphate: an enzyme-bound intermediate in thiamin pyrophosphate-dependent reactions.
    Frey PA.
    Biofactors; 1989 Mar 16; 2(1):1-9. PubMed ID: 2679649
    [Abstract] [Full Text] [Related]

  • 10. The presence of a hydroxyl group at the C-1 atom of the transketolase substrate molecule is necessary for the enzyme to perform the transferase reaction.
    Meshalkina LE, Neef H, Tjaglo MV, Schellenberger A, Kochetov GA.
    FEBS Lett; 1995 Nov 20; 375(3):220-2. PubMed ID: 7498503
    [Abstract] [Full Text] [Related]

  • 11. New function of the amino group of thiamine diphosphate in thiamine catalysis.
    Meshalkina LE, Kochetov GA, Hübner G, Tittmann K, Golbik R.
    Biochemistry (Mosc); 2009 Mar 20; 74(3):293-300. PubMed ID: 19364324
    [Abstract] [Full Text] [Related]

  • 12. Snapshot of a key intermediate in enzymatic thiamin catalysis: crystal structure of the alpha-carbanion of (alpha,beta-dihydroxyethyl)-thiamin diphosphate in the active site of transketolase from Saccharomyces cerevisiae.
    Fiedler E, Thorell S, Sandalova T, Golbik R, König S, Schneider G.
    Proc Natl Acad Sci U S A; 2002 Jan 22; 99(2):591-5. PubMed ID: 11773632
    [Abstract] [Full Text] [Related]

  • 13. [Effect of C-4'-modification of thiamine pyrophosphate on its coenzyme activity in the oxidative decarboxylation of pyruvic acid reaction].
    Severin SE, Khaĭlova LS, Bernkhardt R.
    Ukr Biokhim Zh; 1976 Jan 22; 48(4):503-9. PubMed ID: 982621
    [Abstract] [Full Text] [Related]

  • 14. Which stage of the process of apotransketolase interaction with thiamine diphosphate is affected by the regulatory activity of the donor substrate?
    Esakova OA, Meshalkina LE, Golbik R, Brauer J, Hübner G, Kochetov GA.
    IUBMB Life; 2007 Feb 22; 59(2):104-9. PubMed ID: 17454302
    [Abstract] [Full Text] [Related]

  • 15. [Properties of pig liver transketolase].
    Filippov PP, Shestakova IK, Tikhomirova NK, Kochetov GA.
    Biokhimiia; 1979 Mar 22; 44(3):521-8. PubMed ID: 465597
    [Abstract] [Full Text] [Related]

  • 16. Influence of donor substrate on kinetic parameters of thiamine diphosphate binding to transketolase.
    Ospanov RV, Kochetov GA, Kurganov BI.
    Biochemistry (Mosc); 2007 Jan 22; 72(1):84-92. PubMed ID: 17309441
    [Abstract] [Full Text] [Related]

  • 17. Donor substrate regulation of transketolase.
    Esakova OA, Meshalkina LE, Golbik R, Hübner G, Kochetov GA.
    Eur J Biochem; 2004 Nov 22; 271(21):4189-94. PubMed ID: 15511224
    [Abstract] [Full Text] [Related]

  • 18. The relationship between the thiamin pyrophosphate effect and the saturation status of the transketolase with its coenzyme in human erythrocytes.
    Takeuchi T, Jung EH, Nishino K, Itokawa Y.
    Int J Vitam Nutr Res; 1990 Nov 22; 60(2):112-20. PubMed ID: 2210959
    [Abstract] [Full Text] [Related]

  • 19. Binding of the coenzyme and formation of the transketolase active center.
    Kochetov G, Sevostyanova IA.
    IUBMB Life; 2005 Jul 22; 57(7):491-7. PubMed ID: 16081370
    [Abstract] [Full Text] [Related]

  • 20. [Nature of the bond between the coenzyme and protein in pig liver transketolase].
    Voskoboev AI, Gritsenko EA.
    Biokhimiia; 1981 Aug 22; 46(8):1383-8. PubMed ID: 7272359
    [Abstract] [Full Text] [Related]

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