Paul Cook to Malate Dehydrogenase
This is a "connection" page, showing publications Paul Cook has written about Malate Dehydrogenase.
Connection Strength
3.904
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Role of residues in the adenosine binding site of NAD of the Ascaris suum malic enzyme. Biochim Biophys Acta. 2008 Dec; 1784(12):2059-64.
Score: 0.309
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Proper positioning of the nicotinamide ring is crucial for the Ascaris suum malic enzyme reaction. Biochemistry. 2008 Feb 26; 47(8):2539-46.
Score: 0.298
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Multiple roles of arginine 181 in binding and catalysis in the NAD-malic enzyme from Ascaris suum. Biochemistry. 2007 Dec 18; 46(50):14578-88.
Score: 0.295
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A catalytic triad is responsible for acid-base chemistry in the Ascaris suum NAD-malic enzyme. Biochemistry. 2005 Mar 08; 44(9):3626-35.
Score: 0.244
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Ascaris suum NAD-malic enzyme is activated by L-malate and fumarate binding to separate allosteric sites. Biochemistry. 2003 Aug 19; 42(32):9712-21.
Score: 0.219
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Alternative substrates for malic enzyme: oxidative decarboxylation of L-aspartate. Biochemistry. 2002 Oct 08; 41(40):12200-3.
Score: 0.207
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Lysine 199 is the general acid in the NAD-malic enzyme reaction. Biochemistry. 2000 Oct 03; 39(39):11955-60.
Score: 0.180
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Mapping the active site topography of the NAD-malic enzyme via alanine-scanning site-directed mutagenesis. Biochemistry. 1999 Aug 10; 38(32):10527-32.
Score: 0.166
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Alpha-secondary tritium kinetic isotope effects indicate hydrogen tunneling and coupled motion occur in the oxidation of L-malate by NAD-malic enzyme. Biochemistry. 1999 Apr 06; 38(14):4398-402.
Score: 0.162
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Expression, purification, and characterization of the recombinant NAD-malic enzyme from Ascaris suum. Protein Expr Purif. 1997 Jun; 10(1):51-4.
Score: 0.143
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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. Protein Sci. 1996 Aug; 5(8):1648-54.
Score: 0.135
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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. Biochemistry. 1995 Mar 14; 34(10):3253-60.
Score: 0.122
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Stepwise versus concerted oxidative decarboxylation catalyzed by malic enzyme: a reinvestigation. Biochemistry. 1994 Mar 01; 33(8):2096-103.
Score: 0.114
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Pre-steady-state kinetics reveal a slow isomerization of the enzyme-NAD complex in the NAD-malic enzyme reaction. Biochemistry. 1993 Mar 02; 32(8):1928-34.
Score: 0.106
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Mechanism of activation of the NAD-malic enzyme from Ascaris suum by fumarate. Arch Biochem Biophys. 1992 Dec; 299(2):214-9.
Score: 0.104
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Multiple isotope effects with alternative dinucleotide substrates as a probe of the malic enzyme reaction. Biochemistry. 1991 Jun 11; 30(23):5755-63.
Score: 0.094
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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. Biochemistry. 1991 Jun 11; 30(23):5764-9.
Score: 0.094
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Kinetic mechanism of NAD:malic enzyme from Ascaris suum in the direction of reductive carboxylation. J Biol Chem. 1991 Feb 15; 266(5):2732-8.
Score: 0.092
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Substrate activation by malate induced by oxalate in the Ascaris suum NAD-malic enzyme reaction. Biochemistry. 1989 Jul 25; 28(15):6334-40.
Score: 0.083
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Isotope partitioning for NAD-malic enzyme from Ascaris suum confirms a steady-state random kinetic mechanism. Biochemistry. 1988 Jan 12; 27(1):212-9.
Score: 0.074
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Modification of an arginine residue essential for the activity of NAD-malic enzyme from Ascaris suum. Arch Biochem Biophys. 1987 May 15; 255(1):8-13.
Score: 0.071
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pH dependence of kinetic parameters for oxalacetate decarboxylation and pyruvate reduction reactions catalyzed by malic enzyme. Biochemistry. 1986 Jul 01; 25(13):3752-9.
Score: 0.067
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Protonation mechanism and location of rate-determining steps for the Ascaris suum nicotinamide adenine dinucleotide-malic enzyme reaction from isotope effects and pH studies. Biochemistry. 1986 Jan 14; 25(1):227-36.
Score: 0.065
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Diethylpyrocarbonate inactivation of NAD-malic enzyme from Ascaris suum. Arch Biochem Biophys. 1985 Aug 15; 241(1):67-74.
Score: 0.063
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The pH dependence of the reductive carboxylation of pyruvate by malic enzyme. Biochim Biophys Acta. 1985 Jun 10; 829(2):295-8.
Score: 0.062
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Kinetic mechanism in the direction of oxidative decarboxylation for NAD-malic enzyme from Ascaris suum. Biochemistry. 1984 Nov 06; 23(23):5446-53.
Score: 0.060
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Determination of dissociation constants for enzyme-reactant complexes for NAD-malic enzyme by modulation of the thiol inactivation rate. Biochemistry. 1984 Nov 06; 23(23):5454-9.
Score: 0.060
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Crystallographic studies on Ascaris suum NAD-malic enzyme bound to reduced cofactor and identification of an effector site. J Biol Chem. 2003 Sep 26; 278(39):38051-8.
Score: 0.054
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Crystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 A resolution. Biochemistry. 2002 Jun 04; 41(22):6928-38.
Score: 0.050
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Mechanism from isotope effects. Isotopes Environ Health Stud. 1998; 34(1-2):3-17.
Score: 0.037
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Cloning and nucleotide sequence of a full-length cDNA encoding Ascaris suum malic enzyme. Arch Biochem Biophys. 1993 Jan; 300(1):231-7.
Score: 0.026
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Crystallization of the NAD-dependent malic enzyme from the parasitic nematode Ascaris suum. J Mol Biol. 1992 Jul 20; 226(2):565-9.
Score: 0.025
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pH variation of isotope effects in enzyme-catalyzed reactions. 1. Isotope- and pH-dependent steps the same. Biochemistry. 1981 Mar 31; 20(7):1797-805.
Score: 0.012
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Primary and secondary deuterium isotope effects on equilibrium constants for enzyme-catalyzed reactions. Biochemistry. 1980 Oct 14; 19(21):4853-8.
Score: 0.011