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116 related items for PubMed ID: 8448150

  • 1. Pre-steady-state kinetics reveal a slow isomerization of the enzyme-NAD complex in the NAD-malic enzyme reaction.
    Rajapaksa R, Abu-Soud H, Raushel FM, Harris BG, Cook PF.
    Biochemistry; 1993 Mar 02; 32(8):1928-34. PubMed ID: 8448150
    [Abstract] [Full Text] [Related]

  • 2. Substrate activation by malate induced by oxalate in the Ascaris suum NAD-malic enzyme reaction.
    Park SH, Harris BG, Cook PF.
    Biochemistry; 1989 Jul 25; 28(15):6334-40. PubMed ID: 2790001
    [Abstract] [Full Text] [Related]

  • 3. Protonation mechanism and location of rate-determining steps for the Ascaris suum nicotinamide adenine dinucleotide-malic enzyme reaction from isotope effects and pH studies.
    Kiick DM, Harris BG, Cook PF.
    Biochemistry; 1986 Jan 14; 25(1):227-36. PubMed ID: 3513825
    [Abstract] [Full Text] [Related]

  • 4. Metal ion activator effects on intrinsic isotope effects for hydride transfer from decarboxylation in the reaction catalyzed by the NAD-malic enzyme from Ascaris suum.
    Karsten WE, Gavva SR, Park SH, Cook PF.
    Biochemistry; 1995 Mar 14; 34(10):3253-60. PubMed ID: 7880820
    [Abstract] [Full Text] [Related]

  • 5. Multiple roles of arginine 181 in binding and catalysis in the NAD-malic enzyme from Ascaris suum.
    Karsten WE, Cook PF.
    Biochemistry; 2007 Dec 18; 46(50):14578-88. PubMed ID: 18027982
    [Abstract] [Full Text] [Related]

  • 6. Mechanism of activation of the NAD-malic enzyme from Ascaris suum by fumarate.
    Lai CJ, Harris BG, Cook PF.
    Arch Biochem Biophys; 1992 Dec 18; 299(2):214-9. PubMed ID: 1444459
    [Abstract] [Full Text] [Related]

  • 7. Ascaris suum NAD-malic enzyme is activated by L-malate and fumarate binding to separate allosteric sites.
    Karsten WE, Pais JE, Rao GS, Harris BG, Cook PF.
    Biochemistry; 2003 Aug 19; 42(32):9712-21. PubMed ID: 12911313
    [Abstract] [Full Text] [Related]

  • 8. A catalytic triad is responsible for acid-base chemistry in the Ascaris suum NAD-malic enzyme.
    Karsten WE, Liu D, Rao GS, Harris BG, Cook PF.
    Biochemistry; 2005 Mar 08; 44(9):3626-35. PubMed ID: 15736972
    [Abstract] [Full Text] [Related]

  • 9. Alpha-secondary tritium kinetic isotope effects indicate hydrogen tunneling and coupled motion occur in the oxidation of L-malate by NAD-malic enzyme.
    Karsten WE, Hwang CC, Cook PF.
    Biochemistry; 1999 Apr 06; 38(14):4398-402. PubMed ID: 10194359
    [Abstract] [Full Text] [Related]

  • 10. Metal-Induced reversible structural interconversion of human mitochondrial NAD(P)+-dependent malic enzyme.
    Kuo CW, Hung HC, Tong L, Chang GG.
    Proteins; 2004 Feb 15; 54(3):404-11. PubMed ID: 14747989
    [Abstract] [Full Text] [Related]

  • 11. Kinetic mechanism in the direction of oxidative decarboxylation for NAD-malic enzyme from Ascaris suum.
    Park SH, Kiick DM, Harris BG, Cook PF.
    Biochemistry; 1984 Nov 06; 23(23):5446-53. PubMed ID: 6509028
    [Abstract] [Full Text] [Related]

  • 12. Isotope partitioning for NAD-malic enzyme from Ascaris suum confirms a steady-state random kinetic mechanism.
    Chen CY, Harris BG, Cook PF.
    Biochemistry; 1988 Jan 12; 27(1):212-9. PubMed ID: 3280016
    [Abstract] [Full Text] [Related]

  • 13. Crystallographic studies on Ascaris suum NAD-malic enzyme bound to reduced cofactor and identification of an effector site.
    Rao GS, Coleman DE, Karsten WE, Cook PF, Harris BG.
    J Biol Chem; 2003 Sep 26; 278(39):38051-8. PubMed ID: 12853453
    [Abstract] [Full Text] [Related]

  • 14. Tartrate dehydrogenase catalyzes the stepwise oxidative decarboxylation of D-malate with both NAD and thio-NAD.
    Karsten WE, Tipton PA, Cook PF.
    Biochemistry; 2002 Oct 08; 41(40):12193-9. PubMed ID: 12356321
    [Abstract] [Full Text] [Related]

  • 15. Role of residues in the adenosine binding site of NAD of the Ascaris suum malic enzyme.
    Aktas DF, Cook PF.
    Biochim Biophys Acta; 2008 Dec 08; 1784(12):2059-64. PubMed ID: 18725329
    [Abstract] [Full Text] [Related]

  • 16. Multiple isotope effects with alternative dinucleotide substrates as a probe of the malic enzyme reaction.
    Weiss PM, Gavva SR, Harris BG, Urbauer JL, Cleland WW, Cook PF.
    Biochemistry; 1991 Jun 11; 30(23):5755-63. PubMed ID: 2043615
    [Abstract] [Full Text] [Related]

  • 17. Modification of a thiol at the active site of the Ascaris suum NAD-malic enzyme results in changes in the rate-determining steps for oxidative decarboxylation of L-malate.
    Gavva SR, Harris BG, Weiss PM, Cook PF.
    Biochemistry; 1991 Jun 11; 30(23):5764-9. PubMed ID: 2043616
    [Abstract] [Full Text] [Related]

  • 18. Role of the divalent metal ion in the NAD:malic enzyme reaction: an ESEEM determination of the ground state conformation of malate in the E:Mn:malate complex.
    Tipton PA, Quinn TP, Peisach J, Cook PF.
    Protein Sci; 1996 Aug 11; 5(8):1648-54. PubMed ID: 8844853
    [Abstract] [Full Text] [Related]

  • 19. Determination of the mechanism of human malic enzyme with natural and alternate dinucleotides by isotope effects.
    Rishavy MA, Yang Z, Tong L, Cleland WW.
    Arch Biochem Biophys; 2001 Dec 01; 396(1):43-8. PubMed ID: 11716460
    [Abstract] [Full Text] [Related]

  • 20. Proper positioning of the nicotinamide ring is crucial for the Ascaris suum malic enzyme reaction.
    Aktas DF, Cook PF.
    Biochemistry; 2008 Feb 26; 47(8):2539-46. PubMed ID: 18215074
    [Abstract] [Full Text] [Related]

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