Paul Cook to NAD
This is a "connection" page, showing publications Paul Cook has written about NAD.
Connection Strength
2.577
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Contribution of K99 and D319 to substrate binding and catalysis in the saccharopine dehydrogenase reaction. Arch Biochem Biophys. 2011 Oct; 514(1-2):8-15.
Score: 0.369
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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: 0.301
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Tartrate dehydrogenase catalyzes the stepwise oxidative decarboxylation of D-malate with both NAD and thio-NAD. Biochemistry. 2002 Oct 08; 41(40):12193-9.
Score: 0.201
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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: 0.174
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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: 0.157
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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: 0.131
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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: 0.103
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The oxidation state of active site thiols determines activity of saccharopine dehydrogenase at low pH. Arch Biochem Biophys. 2011 Sep 15; 513(2):71-80.
Score: 0.092
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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: 0.091
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Glutamates 78 and 122 in the active site of saccharopine dehydrogenase contribute to reactant binding and modulate the basicity of the acid-base catalysts. J Biol Chem. 2010 Jul 02; 285(27):20756-68.
Score: 0.085
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Examination of intrinsic sulfonamide resistance in Bacillus anthracis: a novel assay for dihydropteroate synthase. Biochim Biophys Acta. 2008 May; 1780(5):848-53.
Score: 0.073
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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: 0.072
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Determinants of substrate specificity for saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2007 Jun 26; 46(25):7625-36.
Score: 0.069
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Overall kinetic mechanism of saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2006 Oct 03; 45(39):12156-66.
Score: 0.066
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The 2'-phosphate of NADP is responsible for proper orientation of the nicotinamide ring in the oxidative decarboxylation reaction catalyzed by sheep liver 6-phosphogluconate dehydrogenase. J Biol Chem. 2006 Dec 01; 281(48):36803-10.
Score: 0.066
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An isothermal titration calorimetry study of the binding of substrates and ligands to the tartrate dehydrogenase from Pseudomonas putida reveals half-of-the-sites reactivity. Biochemistry. 2006 Jul 25; 45(29):9000-6.
Score: 0.065
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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: 0.063
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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: 0.059
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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: 0.058
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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: 0.058
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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: 0.030
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Stepwise versus concerted oxidative decarboxylation catalyzed by malic enzyme: a reinvestigation. Biochemistry. 1994 Mar 01; 33(8):2096-103.
Score: 0.028
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Product dependence of deuterium isotope effects in enzyme-catalyzed reactions. Biochemistry. 1993 Feb 23; 32(7):1795-802.
Score: 0.026
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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: 0.025
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Evidence in support of lysine 77 and histidine 96 as acid-base catalytic residues in saccharopine dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2012 Jan 31; 51(4):857-66.
Score: 0.024
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Use of primary deuterium and 15N isotope effects to deduce the relative rates of steps in the mechanisms of alanine and glutamate dehydrogenases. Biochemistry. 1988 Jun 28; 27(13):4814-22.
Score: 0.019
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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: 0.018
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Diethylpyrocarbonate inactivation of NAD-malic enzyme from Ascaris suum. Arch Biochem Biophys. 1985 Aug 15; 241(1):67-74.
Score: 0.015
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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: 0.013
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Stereoselective preparation of deuterated reduced nicotinamide adenine nucleotides and substrates by enzymatic synthesis. Anal Biochem. 1979 Jul 15; 96(2):334-40.
Score: 0.010
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Equilibrium model in an in vitro poly(ADP-ribose) turnover system. Biochim Biophys Acta. 1995 Nov 07; 1264(2):201-8.
Score: 0.008
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Kinetic mechanism of dihydropyrimidine dehydrogenase from pig liver. J Biol Chem. 1990 Aug 05; 265(22):12966-72.
Score: 0.005
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Use of isotope effects and pH studies to determine the chemical mechanism of Bacillus subtilis L-alanine dehydrogenase. Biochemistry. 1981 Sep 29; 20(20):5655-61.
Score: 0.003