Paul Cook to Catalysis
This is a "connection" page, showing publications Paul Cook has written about Catalysis.
Connection Strength
2.110
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Evidence for an induced conformational change in the catalytic mechanism of homoisocitrate dehydrogenase for Saccharomyces cerevisiae: Characterization of the D271N mutant enzyme. Arch Biochem Biophys. 2015 Oct 15; 584:20-7.
Score: 0.124
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(31)P NMR spectroscopy senses the microenvironment of the 5'-phosphate group of enzyme-bound pyridoxal 5'-phosphate. Biochim Biophys Acta. 2011 Nov; 1814(11):1447-58.
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: 0.086
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Site-directed mutagenesis as a probe of the acid-base catalytic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2009 Aug 04; 48(30):7305-12.
Score: 0.082
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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: 0.076
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Evidence for a catalytic dyad in the active site of homocitrate synthase from Saccharomyces cerevisiae. Biochemistry. 2008 Jul 01; 47(26):6851-8.
Score: 0.075
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Roles of histidines 154 and 189 and aspartate 139 in the active site of serine acetyltransferase from Haemophilus influenzae. Biochemistry. 2008 Jun 17; 47(24):6322-8.
Score: 0.075
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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: 0.074
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Chemical mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. Biochemistry. 2008 Apr 01; 47(13):4169-80.
Score: 0.074
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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: 0.073
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Proper orientation of the nicotinamide ring of NADP is important for the precatalytic conformational change in the 6-phosphogluconate dehydrogenase reaction. Biochemistry. 2008 Feb 19; 47(7):1862-70.
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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Control of ionizable residues in the catalytic mechanism of tryptophan synthase from Salmonella typhimurium. Biochemistry. 2007 Nov 13; 46(45):13223-34.
Score: 0.072
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Acid-base chemical mechanism of homocitrate synthase from Saccharomyces cerevisiae. Biochemistry. 2006 Oct 03; 45(39):12136-43.
Score: 0.067
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Importance in catalysis of the 6-phosphate-binding site of 6-phosphogluconate in sheep liver 6-phosphogluconate dehydrogenase. J Biol Chem. 2006 Sep 01; 281(35):25568-76.
Score: 0.066
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A three-dimensional homology model of the O-acetylserine sulfhydrylase-B from Salmonella typhimurium. Protein Pept Lett. 2006; 13(1):7-13.
Score: 0.064
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Role of methionine-13 in the catalytic mechanism of 6-phosphogluconate dehydrogenase from sheep liver. Biochemistry. 2005 Feb 22; 44(7):2432-40.
Score: 0.060
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The serine acetyltransferase reaction: acetyl transfer from an acylpantothenyl donor to an alcohol. Arch Biochem Biophys. 2005 Jan 01; 433(1):85-95.
Score: 0.059
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Characterization of the S272A,D site-directed mutations of O-acetylserine sulfhydrylase: involvement of the pyridine ring in the alpha,beta-elimination reaction. Biochemistry. 2003 Jan 14; 42(1):106-13.
Score: 0.052
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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: 0.051
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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: 0.044
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Substitution of pyridoxal 5'-phosphate in D-serine dehydratase from Escherichia coli by cofactor analogues provides information on cofactor binding and catalysis. J Biol Chem. 1999 Dec 24; 274(52):36935-43.
Score: 0.042
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Lysine 183 is the general base in the 6-phosphogluconate dehydrogenase-catalyzed reaction. Biochemistry. 1999 Aug 31; 38(35):11231-8.
Score: 0.041
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Glutamate 190 is a general acid catalyst in the 6-phosphogluconate-dehydrogenase-catalyzed reaction. Biochemistry. 1998 Nov 10; 37(45):15691-7.
Score: 0.039
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Secondary tritium and solvent deuterium isotope effects as a probe of the reaction catalyzed by porcine recombinant dihydropyrimidine dehydrogenase. Biochemistry. 1998 Jun 23; 37(25):9156-9.
Score: 0.038
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Catalytic competence of O-acetylserine sulfhydrylase in the crystal probed by polarized absorption microspectrophotometry. J Mol Biol. 1998; 283(1):135-46.
Score: 0.037
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Time-resolved fluorescence of O-acetylserine sulfhydrylase catalytic intermediates. Biochemistry. 1997 Dec 09; 36(49):15419-27.
Score: 0.036
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A change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst. Biochemistry. 1996 Oct 15; 35(41):13485-93.
Score: 0.034
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Kinetic isotope effects as a probe of the beta-elimination reaction catalyzed by O-acetylserine sulfhydrylase. Biochemistry. 1996 May 21; 35(20):6358-65.
Score: 0.033
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Formation of the alpha-aminoacrylate immediate limits the overall reaction catalyzed by O-acetylserine sulfhydrylase. Biochemistry. 1996 Apr 16; 35(15):4776-83.
Score: 0.032
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Acid-base chemical mechanism of O-acetylserine sulfhydrylases-A and -B from pH studies. Biochemistry. 1995 Sep 26; 34(38):12311-22.
Score: 0.031
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Acid-base catalytic mechanism and pH dependence of fructose 2,6-bisphosphate activation of the Ascaris suum phosphofructokinase. Biochemistry. 1995 Jun 20; 34(24):7781-7.
Score: 0.031
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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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Lanthanide pyrophosphates as substrates for the pyrophosphate-dependent phosphofructokinases from Propionibacterium freudenreichii and Phaseolus aureus: evidence for a second metal ion required for reaction. Biochemistry. 1994 Feb 22; 33(7):1663-7.
Score: 0.028
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Acid-base catalytic mechanism of dihydropyrimidinase from pH studies. Biochemistry. 1993 May 18; 32(19):5160-6.
Score: 0.026
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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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Kinetics of activated thrombin-activatable fibrinolysis inhibitor (TAFIa)-catalyzed cleavage of C-terminal lysine residues of fibrin degradation products and removal of plasminogen-binding sites. J Biol Chem. 2011 Jun 03; 286(22):19280-6.
Score: 0.023
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Haloacetamidine-based inactivators of protein arginine deiminase 4 (PAD4): evidence that general acid catalysis promotes efficient inactivation. Chembiochem. 2010 Jan 25; 11(2):161-5.
Score: 0.021
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Isotope exchange at equilibrium indicates a steady state ordered kinetic mechanism for human sulfotransferase. Biochemistry. 2008 Nov 11; 47(45):11894-9.
Score: 0.019
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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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Glutamate 325 is a general acid-base catalyst in the reaction catalyzed by fructose-2,6-bisphosphatase. Biochemistry. 2000 Dec 26; 39(51):16238-43.
Score: 0.011
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Chemical mechanism of the fructose-6-phosphate,2-kinase reaction from the pH dependence of kinetic parameters of site-directed mutants of active site basic residues. Biochemistry. 1997 Jul 22; 36(29):8775-84.
Score: 0.009
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Solvent isotope effects on the reaction catalyzed by yeast hexokinase. Eur J Biochem. 1983 Aug 15; 134(3):571-4.
Score: 0.003